CD137L, Soluble (mouse) (rec.) Reference: AG-40A-0020Y The CD137 ligand (CD137L; 4-1BBL) is a member of the tumor necrosis factor (TNF) family. CD137L is a type II, transmembrane protein found on activated macrophages, dendritic cells and mature B cells. The interaction with its receptor 4-1BB induces recruitment of TNF receptor-associated factor 1 (TRAF1) and TRAF2 and interaction with the kinase p56lck. CD137 and CD137L have been reported to be involved in tumor rejection, apoptosis, anti-viral immunity, diabetes, in T and B cell co-stimulation and modulation of the immune response.
GITRL, Soluble (human) (rec.) (His) Reference: AG-40A-0024T GITRL (Glucocorticoid-induced TNF receptor ligand) is expressed on dendritic cells (DC), monocytes, macrophages, B cells, activated T cells, endothelial cells, osteoclasts and various healthy non-lymphoid tissues (e.g. testis). GITRL is constitutively expressed and released as soluble form by solid tumors and various hematopoietic malignancies. GITRL causes differentiation of osteoclasts, activation of macrophages, but also alteration of carcinoma and leukemia cells and influences apoptosis. Binding to GITR is important in regulating T cell proliferation and TCR-mediated apoptosis. GITRL is implicated in development of autoimmune diseases and in the immune response against infectious pathogens and tumors.
CD137 (mouse):Fc (human) (rec.) Reference: AG-40A-0025 CD137 (4-1BB) is a member of the tumor necrosis factor (TNF) receptor family. CD137 is expressed by activated T cells, dendritic cells, NK cells, granulocytes and cells of blood vessel walls at sites of inflammation. CD137 has costimulatory activity for activated T cells. Crosslinking of CD137 enhances T cell proliferation, IL-2 secretion survival and cytolytic activity. CD137 was shown to enhance immune activity to eliminate tumors in mice.
IDO (mouse) (rec.) (His) Reference: AG-40A-0030 IDO1 is a heme enzyme that catalyzes the first and rate-limiting step in the main pathway of human tryptophan catabolism, the kynurenine pathway, causing depletion of tryptophan which can lead to halted growth of microbes as well as T cells. IDO1 is an immune checkpoint protein, thought to play a role in a variety of pathophysiological processes such as antimicrobial and antitumor defense, neuropathology, immunoregulation and antioxidant activity. Cancer cells are able to evade the immune system is by hijacking the checkpoint proteins. Increased IDO1 protein levels drive growth arrest and apoptosis of the effector T cells, a group of immune cells that mediate the immune system’s ability to destroy pathogens. By reducing the number of effector T cells, IDO1 overexpression prevents the immune system from effectively destroying cancer cells. IDO1 overexpression has been observed in a wide range of human cancers such as prostatic, colorectal, pancreatic, cervical, gastric, ovarian, head or lung cancer. Physiological IDO1 activity has been implicated in T cell tolerance to tumors, dysfunctional selftolerance in non-obese diabetic (NOD) mice, and as a protective negative regulator in autoimmune disorders.
Nampt (Visfatin/PBEF) (human) (rec.) Reference: AG-40A-0031Y 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. 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.
FABP4 (human) (rec.) (His) Reference: AG-40A-0035 FABP4 is a fatty acid binding protein in adipocytes. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABPs regulate the fatty acid uptake, transport, and metabolism. aP2, the mouse form of FABP4, seems to be central to the pathway that links obesity to insulin resistance. aP2 was shown to be an adipokine linking adipocytes to hepatic glucose production and that neutralizing secreted aP2 may represent an effective therapeutic strategy against diabetes.
GPX3 (human) (rec.) Reference: AG-40A-0037 Glutathione peroxidase 3 (GPX3) is a selenium-dependent extracellular enzyme, protecting cells and enzymes from oxidative damage by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxides. GPX3 is involved in inflammatory bowel disease, in asthma and in diabetes. The activity of GPX3 is significantly reduced in the plasma and tissue of cancer patients. Recently, GPX3 was suggested to serve as a molecular marker for the diagnosis of clear cell type ovarian adenocarcinoma.
FABP1 (human) (rec.) (His) Reference: AG-40A-0039T FABP1 is a fatty acid binding protein in adipocytes. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABPs regulate the fatty acid uptake, transport, and metabolism. FABP1 is required for cholesterol synthesis and metabolism.
RBP4 (human) (rec.) Reference: AG-40A-0041 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.
IL-33 (human) (rec.) (His) Reference: AG-40A-0042 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.
RBP4 (mouse) (rec.) Reference: AG-40A-0045 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 (nuclear form) (human) (rec.) (His) Reference: AG-40A-0047 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.