RBP4 (rat) (rec.) Reference: AG-40A-0049 Retinol binding protein 4 (RBP4; RBP) is a 21kDa secreted protein, a member of the lipocalin family and is known as the primary transporter of retinol (vitamin A) to tissues. A recent report revealed RBP4 as an adipokine linking glucose transporter 4 (GLUT4) suppression in adipose tissue to insulin. Elevated human and mouse serum RBP4 levels are associated with insulin resistance and its severity, obesity, and certain components of metabolic syndrome. Furthermore, human serum RBP4 levels are closely related to renal function.
Clusterin (secretory form) (human) (rec.) Reference: AG-40A-0050Y Clusterin shares homology with the small heat shock protein family of molecular chaperones. The mature secreted form of the protein is a glycosylated, 80kDa disulfide-linked heterodimer of alpha and beta subunits (produced by internal cleavage). Clusterin is expressed in virtually all tissues and found in all human fluids. It is involved in numerous physiological processes important for carcinogenesis and tumor growth, including apoptotic cell death, cell cycle regulation, DNA repair, cell adhesion, tissue remodeling, lipid transportation, membrane recycling and immune system regulation. Clusterin also exists as a nuclear protein. The secreted form of Clusterin has extracellular chaperone and anti-apoptotic activities while the nuclear form acts as a proapoptotic factor.
IL-33 (mouse) (rec.) (His) Reference: AG-40A-0053 Interleukin-33 (IL-33; HF-NEV; IL-1F11), a member of the IL-1 family of cytokines, is expressed by many cell types following pro-inflammatory stimulation and is thought to be released on cell lysis. The 30kDa human IL33 is converted by CASP1 to a 18kDa protein. IL33 binds to and signals through ST2 (IL1R1) and its stimulation recruits MYD88, IRAK, IRAK4, and TRAF6, followed by phosphorylation of ERK1 (MAPK3)/ERK2 (MAPK1), p38 (MAPK14), and JNK. The ability of IL-33 to target numerous immune cell types, like Th2-like cells, mast cells, and B1 cells, and to induce cytokine and chemokine production underlines its potential in influencing the outcome of a wide range of diseases, such as arthritis, asthma, atopic allergy & anaphylaxis, cardiovascular disease/atherosclerosis, nervous system diseases, and sepsis.
Nampt (Visfatin/PBEF) (mouse) (rec.) Reference: AG-40A-0056Y Nicotinamide phosphoribosyltransferase (Nampt; pre-B cell colony-enhancing factor; PBEF; Visfatin) is an adipokine that is localized to the bloodstream and has various functions, including the promotion of vascular smooth muscle cell maturation and inhibition of neutrophil apoptosis. It activates insulin receptor and has insulin-mimetic effects, lowering blood glucose and improving insulin sensitivity. The protein is highly expressed in visceral fat and serum levels of the protein correlate with obesity.
Clusterin (nuclear form) (mouse) (rec.) (His) Reference: AG-40A-0057 Clusterin shares homology with the small heat shock protein family of molecular chaperones. The mature secreted form of the protein is a glycosylated, 80-kDa disulfide-linked heterodimer of alpha and beta subunits (produced by internal cleavage). Clusterin is expressed in virtually all tissues and found in all human fluids. It is involved in numerous physiological processes important for carcinogenesis and tumor growth, including apoptotic cell death, cell cycle regulation, DNA repair, cell adhesion, tissue remodeling, lipid transportation, membrane recycling, and immune system regulation. Clusterin also exists as a nuclear protein. The secreted form of Clusterin has extracellular chaperone and anti-apoptotic activities while the nuclear form acts as a proapoptotic factor.
Nampt (Visfatin/PBEF) (rat) (rec.) Reference: AG-40A-0058 Nicotinamide phosphoribosyltransferase (Nampt; pre-B cell colony-enhancing factor; PBEF; Visfatin) is an 52kDa adipokine secreted by adipose tissue and involved in the biosynthesis of nicotinamide adenine dinucleotide (NAD+). Two forms of Nampt exist, an intracellular form (iNampt) and an extracellular form (eNampt). While the function of iNampt as an essential and rate-limiting NAD+ biosynthetic enzyme is well established, the physiological role of eNampt is still a matter of debate. Nampt has various functions, including the promotion of vascular smooth muscle cell maturation and inhibition of neutrophil apoptosis. It activates insulin receptor and has insulin-mimetic effects, lowering blood glucose and improving insulin sensitivity. The protein is highly expressed in visceral fat and serum levels of the protein correlate with obesity. Recently NAMPT extracellular (eNAMPT) has been shown to be secreted from macrophages in muscles and to triggers a proliferative signal of muscle stem cell (MusC) by binding to CCR5 located at the surface receptor of MusC.
ST2 (human):Fc (human) (rec.) Reference: AG-40A-0059 The ST2 (Interleukin-1 receptor-like 1; Interleukin-33 receptor) gene was originally identified as a gene induced by serum or oncogene expression in fibroblasts. The gene produces a shorter soluble secreted form (ST2) and a longer, transmembrane form (ST2L) by alternative splicing. Soluble ST2 has been shown to downregulate the expression of TLR1 and TLR4. ST2L negatively regulates TLR4 signaling and induces endotoxin tolerance, and enhances Th2 responses. IL-33 is the specific ligand for ST2L.
ANGPTL7 (human) (rec.) Reference: AG-40A-0060 ANGPTL7 (Angiopoietin-like protein 7) is expressed in various tissues and regulates angiogenesis. Human ANGPTL7 was characterized as a potent target gene of the WNT/beta-catenin signaling pathway, and is a pharmacogenomics target in the fields of oncology and regenerative medicine. Overexpression of ANGPTL7 increases collagen expression and might exert a pathogenic role in glaucoma.
Vaspin (human) (rec.) Reference: AG-40A-0064Y Vaspin (Visceral adipose tissue-derived serpin; Serpin A12), a serine protease inhibitor (serpin), is an insulin-sensitizing adipocytokine that has been isolated from both visceral and subcutaneous white adipose tissue. Based on recent findings, vaspin is suggested to regulate immune responses and inflammation and was found to be correlated with various metabolic parameters. Vaspin may represent a novel biomarker for obesity and impaired insulin sensitivity and might serve as a new therapeutic target of metabolic syndrome.
Progranulin (human) (rec.) Reference: AG-40A-0068Y Progranulin (PGRN) is a widely expressed pluripotent growth factor which plays a role in processes such as development, wound repair and inflammation by activating signaling cascades that control cell cycle progression and cell motility. Its function in the central nervous system is of interest, as mutations in the PGRN gene were found in cases of frontotemporal degeneration (FTLD). In addition, PGRN has also been linked to tumorigenesis. Progranulin is a biomarker for FTLD, other types of Alzheimer‘s Disease (AD) and potentially for MCI (Mild Cognitive Impairment). Additionally, PGRN is described as a new ligand of TNF receptors and a potential therapeutic against inflammatory disease like arthritis. EphA2, a member of the large family of Ephrin receptor tyrosine kinases, is also a functional signaling receptor for progranulin as reported recently.
ANGPTL4 (fibrinogen-like domain) (human) (rec.) Reference: AG-40A-0070 ANGPTL4 (Angiopoietin-like protein 4) mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorigenesis and directly regulates lipid, glucose, and energy metabolism. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 is a protein consisting of an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain (FLD). Both domains have distinct biological functions. The coiled-coil domain is responsible for the inhibitory effects on lipoprotein lipase (LPL) converting the active form of LPL into an inactive form, and the FLD domain mediates its antiangiogenic functions. The coiled coil and the FLD domains are separated by a short linker that can be cleaved after secretion. ANGPTL4 appears on the cell surface as the full-length form, where it can be released by heparin treatment. ANGPTL4 protein is then proteolytically cleaved by proprotein convertases (PCs), including furin, PC5/6, paired basic amino acid-cleaving enzyme 4, and PC7.
ANGPTL3 (fibrinogen-like domain) (human) (rec.) Reference: AG-40A-0071Y ANGPTL3 (Angiopoietin-like protein 3) regulates angiogenesis and also directly regulates lipid, glucose and energy metabolism. Angiopoietin-like 3 (ANGPTL3) is a regulator of plasma triglyceride (TRG) levels due to its inhibitory action on the activity of lipoprotein lipase (LPL). ANGPTL3 induces angiogenesis by binding to integrin alphavbeta3. ANGPTL3 is predominantly produced in the liver and can therefore be classified as a hepatokine. In the human plasma, ANGPTL3 is cleaved to release two fragments: a N-terminal coiled-coil domain-containing fragment (aa17-207) important for inhibiting the lipolysis of triglyceride and the C-terminal fibrinogen-like domain-containing fragment (aa208-460).