| Description | Inquire | Purity＞95% SDS-PAGE.FunctionImportant adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing Purity＞95% SDS-PAGE.FunctionImportant adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW.Post-translationalHydroxylated Lys-33 was not identified in PubMed:16497731, probably due to poor representation of the N-terminal peptide in mass fingerprinting. HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagene-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes. O-glycosylated. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：CD200 R1, also known as OX-2 receptor, is a 90 kDa transmembrane protein in the immunoglobulin superfamily and is important in the regulation of myeloid cell activity. The human CD200 R1 cDNA encodes a 325 Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：CD200 R1, also known as OX-2 receptor, is a 90 kDa transmembrane protein in the immunoglobulin superfamily and is important in the regulation of myeloid cell activity. The human CD200 R1 cDNA encodes a 325 amino acid (aa) precursor that includes a 28 aa signal sequence, a 215 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 61 aa cytoplasmic domain. The ECD is composed of one Ig-like V-type domain and one Ig-like C2-type domain. Within the ECD, human CD200 R1 shares 56% aa sequence identity with both mouse and rat CD200 R1. Alternate splicing of the human CD200 R1 mRNA generates four isoforms, two of which are truncated in the Ig-C2 domain and are likely secreted. In human, a separate CD200 RL gene encodes a protein that shares 81% ECD aa identity with CD200 R1. In mouse, at least four genes for CD200 R1-like molecules have been described. CD200 R1 expression is restricted primarily to mast cells, basophils, macrophages, and dendritic cells, while its ligand, CD200, is widely distributed. Disruption of this receptor-ligand system by knockout of the CD200 gene in mice leads to increased macrophage number and activation and predisposition to autoimmune disorders. Association of CD200 with CD200 R1 takes place between their respective N-terminal Ig-like domains. The capacity of CD200 R1-like molecules to interact with CD200 is controversial. CD200 R1 propagates inhibitory signals despite lacking a cytoplasmic ITIM (immunoreceptor tyrosine-based inhibitory motif). CD200 R1-like molecules, in contrast, are potentially activating receptors by means of their association with DAP12. CD200R1 signaling inhibits the expression of proinflammatory molecules including TNFs, IFNs, and inducible nitric oxide synthase in response to selected stimuli, which implicate that CD200/CD200R1 inhibitory signaling pathway plays a prominent role in limiting inflammation in a wide range of inflammatory diseases. Furthermore, the CD200/CD200R inhibitory signaling constitutes one of the most suitable endogenous immunoregulatory molecule candidate to restore the immune suppressive status of the CNS altered in chronic neuroinflammatory situations... Read More | Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description:Cyclophilin B (SCYLP, CyPB, and peptidyl-prolyl cis-trans isomerase B) is a 24 kDa glycoprotein member of the B subfamily of the cyclophilin-type PPIase family of molecules. It is both secreted and retained in Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description:Cyclophilin B (SCYLP, CyPB, and peptidyl-prolyl cis-trans isomerase B) is a 24 kDa glycoprotein member of the B subfamily of the cyclophilin-type PPIase family of molecules. It is both secreted and retained in the ER. When secreted, it mediates chemotaxis and T cell adhesion to fibronectin. This is likely due to its prolyl cis/trans isomerase activity. Intracellularly, Cyclophilin B appears to serve as a molecular chaperone for molecules destined for secretion. It does so via stabilization and facilitating the activity of additional chaperones. The human CyPB precursor is 216 amino acids (aa) in length. It contains a 25 aa signal sequence plus a 191 aa mature region. There is a partial heparin-binding sequence (aa 27‑34), a PPIase domain (aa 47‑204), and a C-terminal ER retention motif (aa 213‑216). Over aa 34‑216, the human and mouse sequences are 95% aa identical... Read More | Purity>98% SDS-PAGE. > 98 % by HPLC.Additional sequence informationThis product is for the mature full length protein. The signal peptide is not included.FunctionCytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including Purity>98% SDS-PAGE. > 98 % by HPLC.Additional sequence informationThis product is for the mature full length protein. The signal peptide is not included.FunctionCytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.BackgroundGM-CSF is a hematopoietic growth factor that stimulates the development of neutrophils and macrophages, and promotes the proliferation and development of early erythroid megakaryocytic and eosinophilic progenitor cells. It is produced by endothelial cells, monocytes, fibroblasts and T-lymphocytes. GM-CSF inhibits neutrophil migration and enhances the functional activity of the mature end-cells. GM-CSF has also been reported to have a functional role on non-hematopoietic cells and can induce human endothelial cells to migrate and proliferate. Additionally, it can stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma and adenocarcinoma cell lines. It is reported that GM-CSF has no biological effects across species. Recombinant Rat GM-CSF is a 14.5kDa globular protein consisting of 127 amino acid residues... Read More |