Cytokines & Chemokines

Vascular Endothelial Growth Factor (VEGF) was initially purified from media conditioned by normal bovine pituitary folliculo-stellate cells and by a variety of transformed cell lines as a mitogen specific for vascular endothelial cells. It was subsequently found to be identical to an independently discovered vascular permeability factor (VPF), which was previously identified in media conditioned by tumor cell lines based on its ability to increase the permeability of capillary blood vessels. Three mouse cDNA clones, which arise through alternative splicing and which encode mature mouse monomeric VEGF having 120, 164, or 188, amino acids, respectively, have been identified. Two receptor tyrosine kinases (RTKs), Flt-1 and Flk-1 (the mouse homologue of human KDR), both members of the type III subclass of RTKs containing seven immunoglobulin-like repeats in their extracellular domains, have been shown to bind VEGF with high affinity. The roles of the homodimers of KDR, Flt, and the heterod

Polypeptide hormones secreted by the parathyroid glands, which promote release of calcium from bone to extracellular fluid by activating osteoblasts and inhibiting osteoclasts, indirectly promote increased intestinal absorption of calcium, and promote renal tubular reabsorption of calcium and increased renal excretion of phosphates. It is a major regulator of bone metabolism. Secretion of parathyroid hormone increases when the level of calcium in the extracellular fluid is low. Its action is opposed by calcitonin.

Polypeptide hormones secreted by the parathyroid glands, which promote release of calcium from bone to extracellular fluid by activating osteoblasts and inhibiting osteoclasts, indirectly promote increased intestinal absorption of calcium, and promote renal tubular reabsorption of calcium and increased renal excretion of phosphates. It is a major regulator of bone metabolism. Secretion of parathyroid hormone increases when the level of calcium in the extracellular fluid is low. Its action is opposed by calcitonin.

MIC-B, Human,50μg

Human High-mobility group box 1 protein (HMGB1), previously known as HMG-1 or amphoterin, is a member of the high mobility group box family of non-histone chromosomal proteins. Human HMGB1 is expressed as a 30 kDa, 215 amino acid (aa) single chain polypeptide containing three domains: two N-terminal globular, 70 aa positively charged DNA-binding domains (HMG boxes A and B), and a negatively charged 30 aa C-terminal region that contains only Asp and Glu.4, 5 Residues 27 - 43 and 178 - 184 contain a NLS. Posttranslational modifications of the molecule have been reported, with acetylation occurring on as many as 17 lysine residues. HMGB1 is expressed at high levels in almost all cells. It was originally discovered as a nuclear protein that could bend DNA. Such bending stabilizes nucleosome formation and regulates the expression of select genes upon recruitment by DNA binding proteins.

Human High-mobility group box 1 protein (HMGB1), previously known as HMG-1 or amphoterin, is a member of the high mobility group box family of non-histone chromosomal proteins. Human HMGB1 is expressed as a 30 kDa, 215 amino acid (aa) single chain polypeptide containing three domains: two N-terminal globular, 70 aa positively charged DNA-binding domains (HMG boxes A and B), and a negatively charged 30 aa C-terminal region that contains only Asp and Glu.4, 5 Residues 27 - 43 and 178 - 184 contain a NLS. Posttranslational modifications of the molecule have been reported, with acetylation occurring on as many as 17 lysine residues. HMGB1 is expressed at high levels in almost all cells. It was originally discovered as a nuclear protein that could bend DNA. Such bending stabilizes nucleosome formation and regulates the expression of select genes upon recruitment by DNA binding proteins.

SPARC, an acronym for ’secreted protein, acidic and rich in cysteine', is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid , 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.

SPARC, an acronym for ’secreted protein, acidic and rich in cysteine', is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid , 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.

Exendin-4 is a novel 39-amino acid peptide isolated from the venom of the Gila monster Heloderma suspectum. It shares 53% sequence homology with GLP-17-36amide and interacts with the same membrane receptor. Exendin-4 enhances glucose-dependent insulin secretion, suppresses inappropriately elevated glucagon secretion, and slows gastric emptying in vivo. It also promotes ß-cell proliferation and neogenesis in vitro and in animal models.