Regardless of the rise in physique fats and weight problems that happens with ageing, there’s a linear lower in meals consumption over the life span. This conundrum is defined by decreased bodily exercise and altered metabolism with ageing. Thus, older individuals fail to adequately regulate meals consumption and develop a physiologic anorexia of ageing.
This physiologic anorexia relies upon not solely on decreased hedonic qualities of feeding with ageing (an space that continues to be controversial) but additionally on altered hormonal and neurotransmitter regulation of meals consumption.
Findings in older animals and people have offered clues to the causes of the anorexia of ageing. A rise in circulating concentrations of the satiating hormone, cholecystokinin, happens with ageing in people. As well as, animal research counsel a lower within the opioid (dynorphin) feeding drive and presumably in neuropeptide Y and nitric oxide.
The physiologic anorexia of ageing places older individuals at excessive threat for creating protein-energy malnutrition after they develop both psychologic or bodily illness processes.
Regardless of its excessive prevalence, nevertheless, protein-energy malnutrition in older individuals is never acknowledged and much more not often handled appropriately. Screening instruments for the early detection of protein-energy malnutrition in older individuals have been developed. A number of treatable causes of pathologic anorexia have been recognized.
There’s growing consciousness of the significance of melancholy as a reason behind extreme weight reduction in older individuals. Approaches to the administration of anorexia and weight reduction in older individuals are reviewed. Though many medication exist that may improve urge for food, none of those are perfect for use in older individuals at the moment.
Description: CXCL4 is a CXC chemokine that is expressed in megakaryocytes and stored in the alpha-granules of platelets. CXCL4 is chemotactic towards neutrophils and monocytes and has been shown to inhibit angiogenesis. Recombinant human CXCL4 is a 7.8 kDa protein containing 70 amino acid residues, including the four highly conserved residues present in CXC chemokines.
Description: CXCL4 is a CXC chemokine that is expressed in megakaryocytes and stored in the alpha-granules of platelets. CXCL4 is chemotactic towards neutrophils and monocytes and has been shown to inhibit angiogenesis. Recombinant human CXCL4 is a 7.8 kDa protein containing 70 amino acid residues, including the four highly conserved residues present in CXC chemokines.
Description: CXCL8 (IL-8) is a proinflammatory CXC chemokine that can signal through the CXCR1 and CXCR2 receptors. It is secreted by monocytes and endothelial cells. CXCL8 (IL-8) chemoattracts and activates neutrophils. Recombinant human CXCL8 (IL-8) (endothelial-derived) is an 8.9 kDa protein containing 77 amino acid residues.
Description: CXCL8 (IL-8) is a proinflammatory CXC chemokine that can signal through the CXCR1 and CXCR2 receptors. It is secreted by monocytes and endothelial cells. CXCL8 (IL-8) chemoattracts and activates neutrophils. Recombinant human CXCL8 (IL-8) (endothelial-derived) is an 8.9 kDa protein containing 77 amino acid residues.
Description: BCMA, a member of the TNF receptor superfamily, binds to BAFF and APRIL. BCMA is expressed on mature B-cells and other B-cell lines and plays an important role in B cell development, function and regulation. BCMA also has the capability to activate NF-kappaB and JNK. The human BCMA gene codes for a 184 amino acid type I transmembrane protein, which contains a 54 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 107 amino acid extracellular domain. Recombinant soluble BCMA is a 50 amino acid polypeptide (5.3 kDa) comprising the TNFR homologous region of the BCMA protein.
Description: BCMA, a member of the TNF receptor superfamily, binds to BAFF and APRIL. BCMA is expressed on mature B-cells and other B-cell lines and plays an important role in B cell development, function and regulation. BCMA also has the capability to activate NF-kappaB and JNK. The human BCMA gene codes for a 184 amino acid type I transmembrane protein, which contains a 54 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 107 amino acid extracellular domain. Recombinant soluble BCMA is a 50 amino acid polypeptide (5.3 kDa) comprising the TNFR homologous region of the BCMA protein.
Description: Visfatin is a 55 kDa protein produced and secreted primarily by white adipose tissue. Recently, Visfatin was isolated from visceral fat deposits and shown to possess insulin-mimetic activity. Like insulin, Visfatin exerts hypoglycemic effects by interacting with the insulin receptor. The binding affinity of Visfatin for the insulin receptor is similar to that of insulin, but it does not compete with insulin, suggesting that the two proteins interact with different receptor sites. The circulating levels of Visfatin are much lower than those of insulin and are not affected by feeding, implying that the hypoglycemic effect of Visfatin may not be of physiological importance. The plasma Visfatin levels, like those of Leptin, correlate positively with the percent of body fat and increase during the development of obesity. Another similarity between Visfatin and Leptin is that their amino acid sequence is highly conserved across different mammalian species and shows no homology to any known protein. Receptors for both Leptin (Ob-R) and Visfatin (i.e. the insulin receptor) are expressed by neurons within the arcuate nucleus of the hypothalamus, a brain area that plays a pivotal role in the regulation of energy metabolism. Although the metabolic function of Visfatin is still unknown, it appears that this newly identified adipocytokine might play an important role, similar to that of Leptin, in the regulation of body weight, i.e. as an afferent signal reflecting excess body fat. Recombinant human Visfatin is a 52.5 kDa protein containing 465 amino acid residues (isoform 1).
Description: Visfatin is a 55 kDa protein produced and secreted primarily by white adipose tissue. Recently, Visfatin was isolated from visceral fat deposits and shown to possess insulin-mimetic activity. Like insulin, Visfatin exerts hypoglycemic effects by interacting with the insulin receptor. The binding affinity of Visfatin for the insulin receptor is similar to that of insulin, but it does not compete with insulin, suggesting that the two proteins interact with different receptor sites. The circulating levels of Visfatin are much lower than those of insulin and are not affected by feeding, implying that the hypoglycemic effect of Visfatin may not be of physiological importance. The plasma Visfatin levels, like those of Leptin, correlate positively with the percent of body fat and increase during the development of obesity. Another similarity between Visfatin and Leptin is that their amino acid sequence is highly conserved across different mammalian species and shows no homology to any known protein. Receptors for both Leptin (Ob-R) and Visfatin (i.e. the insulin receptor) are expressed by neurons within the arcuate nucleus of the hypothalamus, a brain area that plays a pivotal role in the regulation of energy metabolism. Although the metabolic function of Visfatin is still unknown, it appears that this newly identified adipocytokine might play an important role, similar to that of Leptin, in the regulation of body weight, i.e. as an afferent signal reflecting excess body fat. Recombinant human Visfatin is a 52.5 kDa protein containing 465 amino acid residues (isoform 1).
Description: Artemin is a disulfide-linked homodimeric neurotrophic factor structurally related to GDNF, Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. Artemin, GDNF, Persephin and Neurturin all signal through a multicomponent receptor system, composed of RET (receptor tyrosine kinase) and one of the four GFRalpha (alpha1-alpha4) receptors. Artemin prefers the receptor GFRalpha3-RET, but will use other receptors as an alternative. Artemin supports the survival of all peripheral ganglia such as sympathetic, neural crest and placodally derived sensory neurons, and dompaminergic midbrain neurons. The functional human Artemin ligand is a disulfide-linked homodimer, of two 12.0 kDa polypeptide monomers. Each monomer contains seven conserved cysteine residues, one of which is used for interchain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration. Recombinant human Artemin is a 24.2 kDa, disulfide-linked homodimer formed by two identical 113 amino acid subunits.
Description: Artemin is a disulfide-linked homodimeric neurotrophic factor structurally related to GDNF, Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. Artemin, GDNF, Persephin and Neurturin all signal through a multicomponent receptor system, composed of RET (receptor tyrosine kinase) and one of the four GFRalpha (alpha1-alpha4) receptors. Artemin prefers the receptor GFRalpha3-RET, but will use other receptors as an alternative. Artemin supports the survival of all peripheral ganglia such as sympathetic, neural crest and placodally derived sensory neurons, and dompaminergic midbrain neurons. The functional human Artemin ligand is a disulfide-linked homodimer, of two 12.0 kDa polypeptide monomers. Each monomer contains seven conserved cysteine residues, one of which is used for interchain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration. Recombinant human Artemin is a 24.2 kDa, disulfide-linked homodimer formed by two identical 113 amino acid subunits.
Description: Sox2, also known as sex determining region Y (SRY)-box 2, belongs to a diverse family of structurally-related transcription factors whose primary structure contains a 79-residue DNA-binding domain, called high mobility group (HMG) box. It plays an essential role in maintaining the pluripotency of embryonic stem cells (ESC) and determination of cell fate. Microarray analysis showed that Sox2 regulates the expression of multiple genes involved in embryonic development including FGF-4, YES1 and ZFP206. Sox2 acts as a transcriptional activator after forming a ternary complex with Oct3/4 and a conserved non-coding DNA sequence (CNS1) located approximately 2 kb upstream of the RAX promoter. The introduction of Sox2, Oct4, Myc, and Klf4, into human dermal fibroblasts isolated from a skin biopsy of a healthy research fellow was sufficient to confer a pluripotent state upon the fibroblast genome. The reprogrammed cells thus obtained resemble ESC in morphology, gene expression, and in the capacity to form teratomas in immune-deficient mice. Recombinant human Sox2 is a 34.3 kDa protein containing 317 amino-acid residues.
Description: Sox2, also known as sex determining region Y (SRY)-box 2, belongs to a diverse family of structurally-related transcription factors whose primary structure contains a 79-residue DNA-binding domain, called high mobility group (HMG) box. It plays an essential role in maintaining the pluripotency of embryonic stem cells (ESC) and determination of cell fate. Microarray analysis showed that Sox2 regulates the expression of multiple genes involved in embryonic development including FGF-4, YES1 and ZFP206. Sox2 acts as a transcriptional activator after forming a ternary complex with Oct3/4 and a conserved non-coding DNA sequence (CNS1) located approximately 2 kb upstream of the RAX promoter. The introduction of Sox2, Oct4, Myc, and Klf4, into human dermal fibroblasts isolated from a skin biopsy of a healthy research fellow was sufficient to confer a pluripotent state upon the fibroblast genome. The reprogrammed cells thus obtained resemble ESC in morphology, gene expression, and in the capacity to form teratomas in immune-deficient mice. Recombinant human Sox2 is a 34.3 kDa protein containing 317 amino-acid residues.
Description: Nanog is a regulatory protein that is associated with undifferentiated pluripotent cells. The expression of Nanog, which is suppressed in all adult tissues, is restricted to embryonic stem cells and to certain pluripotent cancer cells. Decreased expression of Nanog is strongly correlated with cell differentiation. Nanog, most likely, acts as an intracellular regulator, which maintains pluripotency and self renewal via a STAT3 independent pathway. Recombinant human Nanog is a 34.5 kDa protein, which is synthesized as a 304 amino acid polypeptide lacking a signal sequence for secretion.
Description: Nanog is a regulatory protein that is associated with undifferentiated pluripotent cells. The expression of Nanog, which is suppressed in all adult tissues, is restricted to embryonic stem cells and to certain pluripotent cancer cells. Decreased expression of Nanog is strongly correlated with cell differentiation. Nanog, most likely, acts as an intracellular regulator, which maintains pluripotency and self renewal via a STAT3 independent pathway. Recombinant human Nanog is a 34.5 kDa protein, which is synthesized as a 304 amino acid polypeptide lacking a signal sequence for secretion.
Description: Osteopontin is a secreted glycoprotein that functions as a ligand to alphavbeta3 integrin and possibly other receptors. It binds tightly to hydroxyapatite and can act as a structural component of the extracellular mineralized matrix. Osteopontin is initially secreted as a 298 amino acid protein, which is subject to multiple post-translational modifications including glycosylation, phosphorylation, and specific proteolytic cleavages into various smaller molecular weight fragments. Osteopontin is expressed in a wide range of cells and tissues including osteoblasts, various tumor cell lines, extraosseous cells in the inner ear, brain, kidney, deciduum, placenta and odontoblasts. In addition to its involvement in mineralized matrix formation, Osteopontin can also function as a cytokine that stimulates the release of IFNγ and IL-12, while inhibiting the production of IL-10. Recombinant human Osteopontin is a 298 amino acid protein, which, due to glycosylation, migrates at an apparent molecular weight of 60.0-65.0 kDa by SDS-PAGE analysis under reducing conditions.
Description: Osteopontin is a secreted glycoprotein that functions as a ligand to alphavbeta3 integrin and possibly other receptors. It binds tightly to hydroxyapatite and can act as a structural component of the extracellular mineralized matrix. Osteopontin is initially secreted as a 298 amino acid protein, which is subject to multiple post-translational modifications including glycosylation, phosphorylation, and specific proteolytic cleavages into various smaller molecular weight fragments. Osteopontin is expressed in a wide range of cells and tissues including osteoblasts, various tumor cell lines, extraosseous cells in the inner ear, brain, kidney, deciduum, placenta and odontoblasts. In addition to its involvement in mineralized matrix formation, Osteopontin can also function as a cytokine that stimulates the release of IFNγ and IL-12, while inhibiting the production of IL-10. Recombinant human Osteopontin is a 298 amino acid protein, which, due to glycosylation, migrates at an apparent molecular weight of 60.0-65.0 kDa by SDS-PAGE analysis under reducing conditions.
Description: Neuroserpin is an inhibitory serpin that is expressed predominantly in central nervous system. Although the physiological target of neuroserpin is still unclear, cumulative evidence suggest that it plays an important role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. In the adult brain, neuroserpin is secreted from the growth cones of neurons in areas where synaptic changes are associated with learning and memory, i.e. cerebral cortex, hippocampus, and amygdala. The neuroprotective role of neuroserpin has been demonstrated in transgenic mice lacking neuroserpin expression. The deficiency of neuroserpin in these mice was associated with motor neuron disease characterized by axonal degradation. In humans, defects in neuroserpin, caused by point mutations in the neuroserpin gene, underlie a hereditary disorder called the familial encephalopathy with neuroserpin inclusion bodies (FENIB). Recombinant human neuroserpin is a 44.6 kDa non-glycosylated protein containing 394 amino-acid residues.
Description: Neuroserpin is an inhibitory serpin that is expressed predominantly in central nervous system. Although the physiological target of neuroserpin is still unclear, cumulative evidence suggest that it plays an important role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. In the adult brain, neuroserpin is secreted from the growth cones of neurons in areas where synaptic changes are associated with learning and memory, i.e. cerebral cortex, hippocampus, and amygdala. The neuroprotective role of neuroserpin has been demonstrated in transgenic mice lacking neuroserpin expression. The deficiency of neuroserpin in these mice was associated with motor neuron disease characterized by axonal degradation. In humans, defects in neuroserpin, caused by point mutations in the neuroserpin gene, underlie a hereditary disorder called the familial encephalopathy with neuroserpin inclusion bodies (FENIB). Recombinant human neuroserpin is a 44.6 kDa non-glycosylated protein containing 394 amino-acid residues.
Description: ApoE3 belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. E3 is the most common isoform and is present in 40-90% of the population. Recombinant human ApoE3 is a 34.4 kDa protein containing 300 amino acid residues.
Description: ApoE3 belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. E3 is the most common isoform and is present in 40-90% of the population. Recombinant human ApoE3 is a 34.4 kDa protein containing 300 amino acid residues.
Description: ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Individuals heterozygous for the ApoE4 allele are at higher risk of late-onset Alzheimer’s disease. Recombinant human ApoE4 is a 34.4 kDa protein containing 300 amino acid residues.
Description: ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Individuals heterozygous for the ApoE4 allele are at higher risk of late-onset Alzheimer’s disease. Recombinant human ApoE4 is a 34.4 kDa protein containing 300 amino acid residues.
Description: ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE is an important constituent of all plasma lipoproteins. It’s interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism. It also binds with the LDL receptor (apo B/E). Defects in ApoE are a cause of hyperlipoproteinemia type III. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Compared with E3 and E4, E2 exhibits the lowest receptor binding affinity. E2 allele carriers had significantly lower levels of total cholesterol, low-density lipoprotein cholesterol, and non-high-density lipoprotein cholesterol, as well as increased ApoE levels. Recombinant human ApoE2 is a 34.3 kDa protein containing 300 amino acid residues.
Description: ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE is an important constituent of all plasma lipoproteins. It’s interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism. It also binds with the LDL receptor (apo B/E). Defects in ApoE are a cause of hyperlipoproteinemia type III. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Compared with E3 and E4, E2 exhibits the lowest receptor binding affinity. E2 allele carriers had significantly lower levels of total cholesterol, low-density lipoprotein cholesterol, and non-high-density lipoprotein cholesterol, as well as increased ApoE levels. Recombinant human ApoE2 is a 34.3 kDa protein containing 300 amino acid residues.
Description: CD22 is a B-lineage restricted 135 kDa glycoprotein whose cell surface expression is limited to resting and activated B lymphocytes. The physiological role of CD22 is still unknown. Targeted disruption of CD22 in mice results in a reduced level of surface IgM on peripheral B cells suggesting a role for CD22 in limiting antigen receptor signaling. CD22 is a member of the Ig gene superfamily that uniquely binds a sialic acid-dependent ligand. Recombinant human CD22 is a soluble 75.0 kDa protein which corresponds to the extracellular domain of CD22.
Description: CD22 is a B-lineage restricted 135 kDa glycoprotein whose cell surface expression is limited to resting and activated B lymphocytes. The physiological role of CD22 is still unknown. Targeted disruption of CD22 in mice results in a reduced level of surface IgM on peripheral B cells suggesting a role for CD22 in limiting antigen receptor signaling. CD22 is a member of the Ig gene superfamily that uniquely binds a sialic acid-dependent ligand. Recombinant human CD22 is a soluble 75.0 kDa protein which corresponds to the extracellular domain of CD22.
Description: Epiregulin is an EGF related growth factor that binds specifically to EGFR (ErbB1) and ErbB4, but not ErbB2 or ErbB3. It is expressed mainly in the placenta and peripheral blood leukocytes and in certain carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. It also inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence. Recombinant human Epiregulin is a 5.6 kDa monomeric protein, containing 50 amino residues, which corresponds to the mature secreted Epiregulin sequence.
Description: Epiregulin is an EGF related growth factor that binds specifically to EGFR (ErbB1) and ErbB4, but not ErbB2 or ErbB3. It is expressed mainly in the placenta and peripheral blood leukocytes and in certain carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. It also inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence. Recombinant human Epiregulin is a 5.6 kDa monomeric protein, containing 50 amino residues, which corresponds to the mature secreted Epiregulin sequence.
Description: Prolactin is a neuroendocrine hormone secreted by the pituitary gland. Its primary function is to promote and maintain lactation during pregnancy and suckling. In addition, Prolactin plays an immune-regulatory role by stimulating the activities of ornithine decarboxylase and protein kinase C, which are important for the proliferation, differentiation, and function of lymphocytes. Recombinant human Prolactin is a 23 kDa globular protein containing 200 amino acid residues.
Description: Prolactin is a neuroendocrine hormone secreted by the pituitary gland. Its primary function is to promote and maintain lactation during pregnancy and suckling. In addition, Prolactin plays an immune-regulatory role by stimulating the activities of ornithine decarboxylase and protein kinase C, which are important for the proliferation, differentiation, and function of lymphocytes. Recombinant human Prolactin is a 23 kDa globular protein containing 200 amino acid residues.
Description: PTHrP is a polypeptide hormone produced by almost every tissue of the body. PTHrP is closely related to parathyroid hormone (PTH), which is secreted from the parathyroid gland, and plays a central role in regulating the extracellular concentrations of calcium and phosphorous. Recombinant human PTHrP is a 9.8 kDa linear polypeptide of 86 amino acid residues.
Description: PTHrP is a polypeptide hormone produced by almost every tissue of the body. PTHrP is closely related to parathyroid hormone (PTH), which is secreted from the parathyroid gland, and plays a central role in regulating the extracellular concentrations of calcium and phosphorous. Recombinant human PTHrP is a 9.8 kDa linear polypeptide of 86 amino acid residues.
Description: Keratinocyte Growth Factor (KGF/FGF-7) is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development and postnatal growth and regeneration of variety of tissues, by promoting cellular proliferation and differentiation. KGF/FG-7 is a mitogen factor specific for epithelial cells and keratinocytes and signals through FGFR 2b. KGF/FGF-7 plays a role in kidney and lung development, angiogenesis, and wound healing. Recombinant human KGF/FGF-7 is an 18.9 kDa protein consisting of 163 amino acid residues.
Description: Keratinocyte Growth Factor (KGF/FGF-7) is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development and postnatal growth and regeneration of variety of tissues, by promoting cellular proliferation and differentiation. KGF/FG-7 is a mitogen factor specific for epithelial cells and keratinocytes and signals through FGFR 2b. KGF/FGF-7 plays a role in kidney and lung development, angiogenesis, and wound healing. Recombinant human KGF/FGF-7 is an 18.9 kDa protein consisting of 163 amino acid residues.
Description: VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. Substantial evidence implicates VEGF in the induction of tumor metastasis and intra-ocular neovascular syndromes. VEGF signals through the three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Recombinant human VEGF165 is a 38.2 kDa disulfide-linked homodimeric protein consisting of two 165 amino acid polypeptide chains.
Description: VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. Substantial evidence implicates VEGF in the induction of tumor metastasis and intra-ocular neovascular syndromes. VEGF signals through the three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Recombinant human VEGF165 is a 38.2 kDa disulfide-linked homodimeric protein consisting of two 165 amino acid polypeptide chains.
Description: VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. VEGF signals through three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Due to its increased acidity, VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates. Recombinant human VEGF121 is a 28.4 kDa disulfide-linked homodimeric protein consisting of two 121 amino acid polypeptide chains.
Description: VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. VEGF signals through three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Due to its increased acidity, VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates. Recombinant human VEGF121 is a 28.4 kDa disulfide-linked homodimeric protein consisting of two 121 amino acid polypeptide chains.
Description: HGF is a mesenchymally derived potent mitogen for mature parenchymal hepatocyte cells and acts as a growth factor for a broad spectrum of tissues and cell types. HGF signals through a transmembrane tyrosine kinase receptor known as MET. Activities of HGF include induction of cell proliferation, motility, morphogenesis, inhibition of cell growth, and enhancement of neuron survival. HGF is a crucial mitogen for liver regeneration processes, especially after partial hepatectomy and other liver injuries. Human and murine HGF are cross-reactive. Human HGF is expressed as a linear 697 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of HGF, which consists of two polypeptide chains (α-chain and β-chain) held by a single disulfide bond resulting in formation of a biologically active heterodimer. The α-chain consists of 463 amino acid residues and four kringle domains. The β-chain consists of 234 amino acid residues.
Description: HGF is a mesenchymally derived potent mitogen for mature parenchymal hepatocyte cells and acts as a growth factor for a broad spectrum of tissues and cell types. HGF signals through a transmembrane tyrosine kinase receptor known as MET. Activities of HGF include induction of cell proliferation, motility, morphogenesis, inhibition of cell growth, and enhancement of neuron survival. HGF is a crucial mitogen for liver regeneration processes, especially after partial hepatectomy and other liver injuries. Human and murine HGF are cross-reactive. Human HGF is expressed as a linear 697 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of HGF, which consists of two polypeptide chains (α-chain and β-chain) held by a single disulfide bond resulting in formation of a biologically active heterodimer. The α-chain consists of 463 amino acid residues and four kringle domains. The β-chain consists of 234 amino acid residues.
Description: Members of the Hedgehog (Hh) family are highly conserved proteins which are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh) are structurally related and share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). The biologically active form of Hh molecules is obtained by autocatalytic cleavage of their precursor proteins and corresponds to approximately the N-terminal one half of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can substitute for each other in experimental systems. Recombinant E. coli derived Human Sonic HedgeHog is a 20.0 kDa protein consisting of 176 amino acid residues, including an N-terminal Ile-Val-Ile sequence substituted for the natural occurring chemically modified Cys residue.
Description: Members of the Hedgehog (Hh) family are highly conserved proteins which are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh) are structurally related and share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). The biologically active form of Hh molecules is obtained by autocatalytic cleavage of their precursor proteins and corresponds to approximately the N-terminal one half of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can substitute for each other in experimental systems. Recombinant E. coli derived Human Sonic HedgeHog is a 20.0 kDa protein consisting of 176 amino acid residues, including an N-terminal Ile-Val-Ile sequence substituted for the natural occurring chemically modified Cys residue.
Description: Betacellulin is an EGF-related polypeptide growth factor that signals through the EGF receptor. It is produced in several tissues, including the pancreas, small intestine, and in certain tumor cells. Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Human Betacellulin is initially synthesized as a glycosylated 32.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce the mature sequence. Recombinant human Betacellulin is a 9.0 kDa monomeric protein, containing 80 amino residues, which comprises the mature EGF homologous portion of the Betacellulin protein.
Description: Betacellulin is an EGF-related polypeptide growth factor that signals through the EGF receptor. It is produced in several tissues, including the pancreas, small intestine, and in certain tumor cells. Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Human Betacellulin is initially synthesized as a glycosylated 32.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce the mature sequence. Recombinant human Betacellulin is a 9.0 kDa monomeric protein, containing 80 amino residues, which comprises the mature EGF homologous portion of the Betacellulin protein.
Description: Epigen is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. It is produced in several tissues, including the testis, liver, heart and in certain tumor cells. Epigen is mitogenic for fibroblasts and epithelial cells. Human Epigen is initially synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence. Recombinant human Epigen is a 7.9kDa monomeric protein, containing 72 amino acid residues, which comprises the EGF homologous portion of the Epigen precursor.
Description: Epigen is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. It is produced in several tissues, including the testis, liver, heart and in certain tumor cells. Epigen is mitogenic for fibroblasts and epithelial cells. Human Epigen is initially synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence. Recombinant human Epigen is a 7.9kDa monomeric protein, containing 72 amino acid residues, which comprises the EGF homologous portion of the Epigen precursor.
Description: Klotho is a glycosylated protein that plays an important role in the regulation of phosphate and calcium homeostasis. The full length transmembrane form has a large extracellular domain composed of two homologous subunits termed KL1 and KL2, which contain 516 and 439 amino acid residues, respectively, The predominant circulating form, which is derived from alternative RNA splicing, contains the KL1 subunit and constitutes the N-terminal sequence of transmembrane Klotho. A third Klotho protein of about 128 kDa has been identified in the blood and cerebrospinal fluid. This circulating protein arises from the action of an as yet unidentified protease which cleaves transmembrane Klotho just above and/or within the plasma membrane. Klotho has been shown to play a key role in the signaling cascade of fibroblast growth factor-23 (FGF-23), a bone derived hormone that acts in the kidney to inhibit phosphate reabsorption and vitamin D biosynthesis. Klotho promotes FGF-23 signaling through binding to FGFRI (IIIc) which converts this canonical FGF receptor into a specific receptor for FGF-23. In the absence of Klotho the function of FGF-23 is literally abolished. Recombinant human Klotho is a 65-70 kDa glycoprotein containing 516 amino acid residues.
Description: Klotho is a glycosylated protein that plays an important role in the regulation of phosphate and calcium homeostasis. The full length transmembrane form has a large extracellular domain composed of two homologous subunits termed KL1 and KL2, which contain 516 and 439 amino acid residues, respectively, The predominant circulating form, which is derived from alternative RNA splicing, contains the KL1 subunit and constitutes the N-terminal sequence of transmembrane Klotho. A third Klotho protein of about 128 kDa has been identified in the blood and cerebrospinal fluid. This circulating protein arises from the action of an as yet unidentified protease which cleaves transmembrane Klotho just above and/or within the plasma membrane. Klotho has been shown to play a key role in the signaling cascade of fibroblast growth factor-23 (FGF-23), a bone derived hormone that acts in the kidney to inhibit phosphate reabsorption and vitamin D biosynthesis. Klotho promotes FGF-23 signaling through binding to FGFRI (IIIc) which converts this canonical FGF receptor into a specific receptor for FGF-23. In the absence of Klotho the function of FGF-23 is literally abolished. Recombinant human Klotho is a 65-70 kDa glycoprotein containing 516 amino acid residues.
Description: Myostatin is a TGF-beta family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the Activin-binding protein Follistatin, and by the propeptide of Myostatin. Recombinant Human myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond.
Description: Myostatin is a TGF-beta family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the Activin-binding protein Follistatin, and by the propeptide of Myostatin. Recombinant Human myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond.
Description: Twisted Gastrulation Protein (TSG) is a secreted BMP binding protein structurally related to the BMP antagonists Chordin and Noggin. TSG can inhibit BMP activity by binding directly to BMP proteins, and can act either as a BMP4 agonist or antagonist (depending on the specific biochemical environment) by binding to the BMP4/Chordin complex. Recombinant human TSG is a 199 amino acid 22.2 kDa protein containing the BMP/TGFβ binding portion of the full length TSG protein.
Description: Twisted Gastrulation Protein (TSG) is a secreted BMP binding protein structurally related to the BMP antagonists Chordin and Noggin. TSG can inhibit BMP activity by binding directly to BMP proteins, and can act either as a BMP4 agonist or antagonist (depending on the specific biochemical environment) by binding to the BMP4/Chordin complex. Recombinant human TSG is a 199 amino acid 22.2 kDa protein containing the BMP/TGFβ binding portion of the full length TSG protein.
Description: Noggin belongs to a group of diffusible proteins which bind to ligands of the TGF-β family and regulate their activity by inhibiting their access to signaling receptors. The interplay between TGF-β ligands and their natural antagonists has major biological significance during development processes, in which cellular response can vary considerably depending upon the local concentration of the signaling molecule. Noggin was originally identified as a BMP-4 antagonist whose action is critical for proper formation of the head and other dorsal structures. Consequently, Noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of Noggin in mice results in prenatal death and recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing Noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant human Noggin is a 46 kDa disulfide-linked homodimer (120-10C) consisting of two 206 amino acid polypeptide chains. Monomeric glycosylated Noggin migrates at an apparent molecular weight of approximately 28.0-33.0 kDa by SDS PAGE analysis under reducing conditions.
Description: Noggin belongs to a group of diffusible proteins which bind to ligands of the TGF-β family and regulate their activity by inhibiting their access to signaling receptors. The interplay between TGF-β ligands and their natural antagonists has major biological significance during development processes, in which cellular response can vary considerably depending upon the local concentration of the signaling molecule. Noggin was originally identified as a BMP-4 antagonist whose action is critical for proper formation of the head and other dorsal structures. Consequently, Noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of Noggin in mice results in prenatal death and recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing Noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant human Noggin is a 46 kDa disulfide-linked homodimer (120-10C) consisting of two 206 amino acid polypeptide chains. Monomeric glycosylated Noggin migrates at an apparent molecular weight of approximately 28.0-33.0 kDa by SDS PAGE analysis under reducing conditions.
Description: Follistatin is a secreted protein that binds to ligands of the TGF-β family and regulates their activity by inhibiting their access to signaling receptors. It was originally discovered as activin antagonists whose activity suppresses expression and secretion of the pituitary hormone FSH (follicle stimulating hormone). In addition to being a natural antagonist, follistatin can inhibit the activity of other TGF-β ligands including BMP-2,-4,-6,-7, Myostatin, GDF-11, and TGF-β1. Follistatin is expressed in the pituitary, ovaries, decidual cells of the endometrium, and in some other tissues. Recombinant human Follistatin is a 31.5 kDa protein containing 288 amino acids. Its primary structure contains three cysteine-rich domains (called FS domains), each followed by a protease-inhibitory kazal domain.
Description: Follistatin is a secreted protein that binds to ligands of the TGF-β family and regulates their activity by inhibiting their access to signaling receptors. It was originally discovered as activin antagonists whose activity suppresses expression and secretion of the pituitary hormone FSH (follicle stimulating hormone). In addition to being a natural antagonist, follistatin can inhibit the activity of other TGF-β ligands including BMP-2,-4,-6,-7, Myostatin, GDF-11, and TGF-β1. Follistatin is expressed in the pituitary, ovaries, decidual cells of the endometrium, and in some other tissues. Recombinant human Follistatin is a 31.5 kDa protein containing 288 amino acids. Its primary structure contains three cysteine-rich domains (called FS domains), each followed by a protease-inhibitory kazal domain.
Description: CTGFL/WISP-2 is a 24.3 kDa protein that belongs to the CCN family of cysteine rich regulatory proteins. Members of this family stimulate mitosis, adhesion, apoptosis, extracellular matrix production, growth arrest, and migration of multiple cell types. The protein is expressed in primary osteoblasts, fibroblasts, ovary, testes, and heart. In addition to promoting adhesion of osteoblasts, CTGFL/WISP-2 inhibits osteocalcin production, as well as binding of fibrinogen to integrin receptors. Recombinant human CTGFL/WISP-2 is a 24.3 kDa protein of 228 amino acid residues.
Description: CTGFL/WISP-2 is a 24.3 kDa protein that belongs to the CCN family of cysteine rich regulatory proteins. Members of this family stimulate mitosis, adhesion, apoptosis, extracellular matrix production, growth arrest, and migration of multiple cell types. The protein is expressed in primary osteoblasts, fibroblasts, ovary, testes, and heart. In addition to promoting adhesion of osteoblasts, CTGFL/WISP-2 inhibits osteocalcin production, as well as binding of fibrinogen to integrin receptors. Recombinant human CTGFL/WISP-2 is a 24.3 kDa protein of 228 amino acid residues.
Description: CTGF is a member of the CCN family of secreted cysteine rich regulatory proteins and is the major mitogenic and chemoattractant protein produced by umbilical vein and vascular endothelial cells. CTGF stimulates the proliferation and differentiation of chondrocytes, induces angiogenesis, promotes cell adhesion of fibroblasts, endothelial, and epithelial cells, and binds to IGF, TGF beta1, and BMP-4. Cell migration and adhesion are signaled through binding to specific cell surface integrins and to heparin sulfate proteoglycans CTGF (98 a.a.), a lower molecular weight isoform containing the C-terminal portion of the full length CTGF protein, exerts full heparin binding, cell adhesion, and mitogenic CTGF activity. Recombinant human CTGF is a 11.2 kDa protein of 98 amino acid residues.
Description: CTGF is a member of the CCN family of secreted cysteine rich regulatory proteins and is the major mitogenic and chemoattractant protein produced by umbilical vein and vascular endothelial cells. CTGF stimulates the proliferation and differentiation of chondrocytes, induces angiogenesis, promotes cell adhesion of fibroblasts, endothelial, and epithelial cells, and binds to IGF, TGF beta1, and BMP-4. Cell migration and adhesion are signaled through binding to specific cell surface integrins and to heparin sulfate proteoglycans CTGF (98 a.a.), a lower molecular weight isoform containing the C-terminal portion of the full length CTGF protein, exerts full heparin binding, cell adhesion, and mitogenic CTGF activity. Recombinant human CTGF is a 11.2 kDa protein of 98 amino acid residues.
Description: CYR61 is a member of the CCN family of secreted cysteine rich regulatory proteins. CYR61 induces angiogenesis by stimulating the proliferation, migration, and adhesion of endothelial cells. Cell migration and adhesion are mediated through binding to specific cell surface integrins and to heparin sulfate proteoglycans. Increased expression of CYR61 is associated with several types of cancer, and correlates with the progression and estrogen independence of human breast cancers. Recombinant human CYR61 is a 39.5 kDa protein containing 357 amino acid residues. It is composed of four distinct structural domains (modules); the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the Thrombospondin type-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).
Description: CYR61 is a member of the CCN family of secreted cysteine rich regulatory proteins. CYR61 induces angiogenesis by stimulating the proliferation, migration, and adhesion of endothelial cells. Cell migration and adhesion are mediated through binding to specific cell surface integrins and to heparin sulfate proteoglycans. Increased expression of CYR61 is associated with several types of cancer, and correlates with the progression and estrogen independence of human breast cancers. Recombinant human CYR61 is a 39.5 kDa protein containing 357 amino acid residues. It is composed of four distinct structural domains (modules); the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the Thrombospondin type-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).
Description: NOV is a member of the CCN family of secreted cysteine rich regulatory proteins. The full length NOV protein contains four structural domains that confer distinct, and sometimes opposing, biological activities. Elevated expression of NOV is associated with certain tumors, including Wilm’s tumor and most nephroblastomas. However, in other tumor types and certain cancer cell lines, increased tumorgenicity and proliferation is correlated with decreased NOV expression. Additionally, NOV induces cell adhesion and cell migration by signaling through specific cell surface integrins and by binding to heparin sulfate proteoglycans and to fibulin 1C. NOV has also been reported to exert proangiogenic activities. Recombinant human NOV is a 36.2 kDa protein containing 331 amino acid residues. It is composed of four distinct structural domains (modules); the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the Thrombospondin type-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).
Description: NOV is a member of the CCN family of secreted cysteine rich regulatory proteins. The full length NOV protein contains four structural domains that confer distinct, and sometimes opposing, biological activities. Elevated expression of NOV is associated with certain tumors, including Wilm’s tumor and most nephroblastomas. However, in other tumor types and certain cancer cell lines, increased tumorgenicity and proliferation is correlated with decreased NOV expression. Additionally, NOV induces cell adhesion and cell migration by signaling through specific cell surface integrins and by binding to heparin sulfate proteoglycans and to fibulin 1C. NOV has also been reported to exert proangiogenic activities. Recombinant human NOV is a 36.2 kDa protein containing 331 amino acid residues. It is composed of four distinct structural domains (modules); the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the Thrombospondin type-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).
Description: MIA is the first discovered member of a family of secreted cytokines termed the MIA/OTOR family. The four known members of this family; MIA, MIA2, OTOR and TANGO each contain a Src homology-3 (SH3)-like domain. MIA is an autocrine growth regulatory protein secreted from chondrocytes and malignant melanoma cells that promotes melanoma metastasis by binding competitively to fibronectin and laminin in a manner that results in melanoma cell detachment from the extracellular matrix in vivo. Elevated levels of MIA may represent a clinically useful marker for diagnosis of melanoma metastasis as well as a potential marker for rheumatoid arthritis. Recombinant human MIA is a 12.2 kDa globular protein containing 108 amino acid residues including two intramolecular disulfide bonds.
Description: MIA is the first discovered member of a family of secreted cytokines termed the MIA/OTOR family. The four known members of this family; MIA, MIA2, OTOR and TANGO each contain a Src homology-3 (SH3)-like domain. MIA is an autocrine growth regulatory protein secreted from chondrocytes and malignant melanoma cells that promotes melanoma metastasis by binding competitively to fibronectin and laminin in a manner that results in melanoma cell detachment from the extracellular matrix in vivo. Elevated levels of MIA may represent a clinically useful marker for diagnosis of melanoma metastasis as well as a potential marker for rheumatoid arthritis. Recombinant human MIA is a 12.2 kDa globular protein containing 108 amino acid residues including two intramolecular disulfide bonds.
Description: OTOR, also called Otoraplin and MIAL, is a secreted cytokine and a member of the MIA/OTOR family. Members of this family which also includes MIA, MIA2, and TANGO share a Src homology-3 (SH3)-like domain. OTOR is predominantly expressed in the cochlea of the inner-ear and to a lesser extent in fetal brain and in some cartilage tissues. OTOR appears to be involved in early chondrogenesis of the otic capsule, which is required for normal inner ear development and auditory function. Recombinant human OTOR is a 12.7 kDa globular protein containing 112 amino acid residues.
Description: OTOR, also called Otoraplin and MIAL, is a secreted cytokine and a member of the MIA/OTOR family. Members of this family which also includes MIA, MIA2, and TANGO share a Src homology-3 (SH3)-like domain. OTOR is predominantly expressed in the cochlea of the inner-ear and to a lesser extent in fetal brain and in some cartilage tissues. OTOR appears to be involved in early chondrogenesis of the otic capsule, which is required for normal inner ear development and auditory function. Recombinant human OTOR is a 12.7 kDa globular protein containing 112 amino acid residues.
Description: Vaspin is a newly described adipocytokine expressed predominantly in visceral white adipose tissues. Structure analysis of Vaspin predicts the presence of three β-sheets, nine α-helices, and one central loop, which are distinctive structural features of Serpin family members. The serpins are irreversible ("suicidal”) serine-protease inhibitors, characterized by having more than 30% sequence homology with α1-antitrypsin and a conserved tertiary structure, which contains an exposed reactive center loop that acts as a pseudo-substrate for the target proteinase. Members of this family play an important role in a number of fundamental biological processes including blood coagulation, fibrinolysis, complement activation, angiogenesis, inflammation, and tumor suppression. In human, the serpins represent approximately 2% of total serum proteins, of which 70% is α1- antitrypsin. Vaspin exhibits 40.2% sequence identity with α-1-antitrypsin. Yet, its protease inhibitory activity is still unknown. Vaspin mRNA expression in visceral fat is positively correlated with BMI and percent of body fat. Administration of Vaspin to obese mice improved glucose tolerance and insulin sensitivity, reflected by normalized blood glucose levels. It also led to the reversal of altered expression of diabetes-relevant adipocytokines including leptin, adiponectin, resistin, and TNF-α. These findings suggest a potential clinical use for Vaspin in ameliorating certain aberrations seen in the diabetic/obesity metabolic syndrome. Recombinant human Vaspin is a 45.2 kDa protein containing 395 amino-acid residues.
Description: Vaspin is a newly described adipocytokine expressed predominantly in visceral white adipose tissues. Structure analysis of Vaspin predicts the presence of three β-sheets, nine α-helices, and one central loop, which are distinctive structural features of Serpin family members. The serpins are irreversible ("suicidal”) serine-protease inhibitors, characterized by having more than 30% sequence homology with α1-antitrypsin and a conserved tertiary structure, which contains an exposed reactive center loop that acts as a pseudo-substrate for the target proteinase. Members of this family play an important role in a number of fundamental biological processes including blood coagulation, fibrinolysis, complement activation, angiogenesis, inflammation, and tumor suppression. In human, the serpins represent approximately 2% of total serum proteins, of which 70% is α1- antitrypsin. Vaspin exhibits 40.2% sequence identity with α-1-antitrypsin. Yet, its protease inhibitory activity is still unknown. Vaspin mRNA expression in visceral fat is positively correlated with BMI and percent of body fat. Administration of Vaspin to obese mice improved glucose tolerance and insulin sensitivity, reflected by normalized blood glucose levels. It also led to the reversal of altered expression of diabetes-relevant adipocytokines including leptin, adiponectin, resistin, and TNF-α. These findings suggest a potential clinical use for Vaspin in ameliorating certain aberrations seen in the diabetic/obesity metabolic syndrome. Recombinant human Vaspin is a 45.2 kDa protein containing 395 amino-acid residues.
Description: Maspin (mammary serine protease inhibitor) is a non-inhibitory serpin that is expressed predominantly in normal mammary epithelial cells but at significantly reduced levels or absent in most breast carcinomas. It has the ability to block the growth, invasiveness, and metastatic potential of breast and lung tumors. This anti-tumor activity is achieved, in part, by the ability of Maspin to inhibit angiogenesis and to preferentially promote apoptosis of tumor cells. Recombinant human Maspin is a 42.2 kDa non-glycosylated protein containing 375 amino acid residues.
Description: Maspin (mammary serine protease inhibitor) is a non-inhibitory serpin that is expressed predominantly in normal mammary epithelial cells but at significantly reduced levels or absent in most breast carcinomas. It has the ability to block the growth, invasiveness, and metastatic potential of breast and lung tumors. This anti-tumor activity is achieved, in part, by the ability of Maspin to inhibit angiogenesis and to preferentially promote apoptosis of tumor cells. Recombinant human Maspin is a 42.2 kDa non-glycosylated protein containing 375 amino acid residues.
Description: PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is a 50 kDa glycoprotein produced and secreted in many tissues throughout the body. A major component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. In addition, PEDF is able to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuroprotective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recent identification of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity (1) should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities implicate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF also has the potential to be useful in the treatment of various angiogenesis-related diseases including a number of cancers. Recombinant PEDF is a 44.5 kDa non-glycosylated protein containing 400 amino acid residues. (1) Notari, I. et al. J Biol Chem., Vol. 281, 38022-38037.
Description: PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is a 50 kDa glycoprotein produced and secreted in many tissues throughout the body. A major component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. In addition, PEDF is able to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuroprotective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recent identification of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity (1) should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities implicate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF also has the potential to be useful in the treatment of various angiogenesis-related diseases including a number of cancers. Recombinant PEDF is a 44.5 kDa non-glycosylated protein containing 400 amino acid residues. (1) Notari, I. et al. J Biol Chem., Vol. 281, 38022-38037.
Description: Endostatin is a naturally occurring 20 kDa polypeptide derived from the C-terminal portion of type XVIII collagen. It functions as an anti-angiogenic cytokine that is expressed in various organs with the highest levels in liver, lung and kidney. Endostatin inhibits angiogenesis by blocking the pro-angiogenic activities of VEGF and FGF-basic. Recombinant human Endostatin is a 20.2 kDa protein consisting 184 amino acid residues.
Description: Endostatin is a naturally occurring 20 kDa polypeptide derived from the C-terminal portion of type XVIII collagen. It functions as an anti-angiogenic cytokine that is expressed in various organs with the highest levels in liver, lung and kidney. Endostatin inhibits angiogenesis by blocking the pro-angiogenic activities of VEGF and FGF-basic. Recombinant human Endostatin is a 20.2 kDa protein consisting 184 amino acid residues.
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Irritation in end-stage renal disease–what have we discovered in 10 years?
The primary experiences connecting uremic irritation with a wasted and atherogenic phenotype and poor final result initiated within the late 1990s. Since then, about 3500 publications seem on Medline, reflecting the exponential curiosity that this matter has evoked in nephrology.
What was described as a “novel” threat issue 10 years in the past has now developed into a longtime discovering in sufferers with end-stage renal illness (ESRD). The aim of this evaluation is to summarize the primary advances contributing to our present understanding of the complicated inflammatory processes current in ESRD.
Causes and penalties of irritation, genetic heritability of the inflammatory response, implications on final result prognostication, and modern therapeutic proof are a few of the numerous subjects mentioned.
Prenatal malnutrition and growth of the mind.
On this evaluation, we’ve summarized numerous points as to how prenatal protein malnutrition impacts growth of the mind and have tried to combine a number of broad rules, ideas, and developments on this discipline in relation to our findings and different research of malnutrition insults.
Diet might be the only best environmental affect each on the fetus and neonate, and performs a mandatory position within the maturation and purposeful growth of the central nervous system.
Prenatal protein malnutrition adversely impacts the creating mind in quite a few methods, relying largely on its timing in relation to numerous developmental occasions within the mind and, to a lesser extent, on the kind and severity of the deprivation.
Most of the results of prenatal malnutrition are everlasting, although some extent of amelioration could also be produced by publicity to stimulating and enriched environments. Malnutrition exerts its results throughout growth, not solely through the so-called mind development spurt interval, but additionally throughout early organizational processes akin to neurogenesis, cell migration, and differentiation.
Malnutrition ends in quite a lot of minimal mind dysfunction-type syndromes and in the end impacts attentional processes and interactions of the organism with the atmosphere, specifically producing purposeful isolation from the atmosphere, usually main to varied kinds of studying disabilities.
In malnutrition insult, we’re coping with a distributed, not focal, mind pathology and numerous developmental failures. Quantitative evaluations present distorted relations between neurons and glia, poor formation of neuronal circuits and alterations of regular regressive occasions, together with cell loss of life and axonal and dendritic pruning, leading to modified patterns of mind group.
Malnutrition insult ends in deviations in regular age-related sequences of mind maturation, significantly affecting coordinated growth of varied cell varieties and, in the end, affecting the formation of neuronal circuits and the commencing of exercise of neurotransmitter cell varieties and, in the end, affecting the formation of neuronal circuits and the commencing of exercise of neurotransmitter programs.
It’s apparent that such diffuse sort “lesions” will be adequately assessed solely by interdisciplinary research throughout a broad vary of approaches, together with morphological, biochemical, neurophysiological, and behavioral analyses.
Description: A polyclonal antibody raised in Chicken that recognizes and binds to Human P-Zero Myelin Protein (Pz0) . This antibody is tested and proven to work in the following applications:
Description: A polyclonal antibody raised in Goat that recognizes and binds to Human Goat Anti-Myelin Protein zero . This antibody is tested and proven to work in the following applications:
Myelin Protein Zero-Like Protein 1 (MPZL1) Antibody
Description: Qualitativeindirect ELISA kit for measuring Human myelin protein zero antibody (IgG) in samples from serum, plasma. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price.
Description: Qualitativeindirect ELISA kit for measuring Human myelin protein zero antibody(IgG) in samples from serum, plasma. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits.
Description: Quantitativesandwich ELISA kit for measuring Human myelin protein zero antibody (IgM) in samples from serum, plasma, cell culture supernates, tissue homogenates. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price.
Description: Quantitativesandwich ELISA kit for measuring Human myelin protein zero antibody(IgM) in samples from serum, plasma, cell culture supernates, tissue homogenates. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits.
Description: Quantitativesandwich ELISA kit for measuring Rat myelin protein zero (p0) in samples from serum, plasma, tissue homogenates, cell lysates. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price.
Description: Quantitativesandwich ELISA kit for measuring Rat myelin protein zero (p0) in samples from serum, plasma, tissue homogenates, cell lysates. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits.
Description: A sandwich quantitative ELISA assay kit for detection of Human Protein Zero, Myelin (MPZ) in samples from tissue homogenates, cell lysates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Human Protein Zero, Myelin (MPZ) in samples from tissue homogenates, cell lysates or other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Protein Zero, Myelin (MPZ) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Protein Zero, Myelin (MPZ) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Protein Zero, Myelin (MPZ) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Protein Zero, Myelin (MPZ) in tissue homogenates, cell lysates and other biological fluids.
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Protein Zero, Myelin (MPZ) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Protein Zero, Myelin (MPZ) in Tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Protein Zero, Myelin (MPZ) in Tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Protein Zero, Myelin (MPZ) in Tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Protein Zero, Myelin (MPZ) in Tissue homogenates, cell lysates and other biological fluids.
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Rat Protein Zero, Myelin (MPZ) in samples from Tissue homogenates, cell lysates and other biological fluids. with no significant corss-reactivity with analogues from other species.
Description: A sandwich ELISA kit for detection of Protein Zero, Myelin from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids.
Description: A sandwich ELISA kit for detection of Protein Zero, Myelin from Rat in samples from blood, serum, plasma, cell culture fluid and other biological fluids.
Description: Quantitative sandwich ELISA for measuring Rat Myelin protein zero (MPZ) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
Description: Quantitative sandwich ELISA for measuring Rat Myelin protein zero (MPZ) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
Controlling Phosphorus By Decreasing Dietary Protein Intake Beneficial or Harmful
Is controlling phosphorus by lowering dietary protein consumption helpful or dangerous in individuals with continual kidney illness? BACKGROUND Dietary restrictions...
