Anti-Alpha 1 microglobulin / AMBP / Bikunin, clone AMBP/4536

1 mg/ml in 1X PBS, BSA free, sodium azide free. The AMBP (Alpha-1-Microglobulin/Bikunin precursor) gene encodes a protein precursor, known as AMBP, that is cleaved to produce two distinct proteins, designated Alpha-1-Microglobulin and Bikunin. Alpha-1-Microglobulin, also known as protein HC, is a member of the lipocalin superfamily and is secreted mainly in plasma, urine and cerebrospinal fluid. Thought to have reductase/dehydrogenase activity, Alpha-1-Microglobulin exhibits immunosuppressive properties, such as cytokine secretion and inhibition of antigen-induced lymphocyte cell proliferation, and may be involved in the reduction of biological pro-oxidants. The second protein cleavage product, designated Bikunin and also known as inter-Alpha-trypsin inhibitor light chain, ITI-LC or urinary trypsin inhibitor, is a widely expressed protein that is stored in the granules of human connective tissue mast cells. One of many proteins in the Kunitz-type protease inhibitor family, Bikunin prevents autodigestion by exocrine enzymes, such as trypsinogen and chymo-trypsinogen, and plays a role in the antiinflammatory/antiproteinase immune response. Unlike Alpha-1-Microglobulin, Bikunin is implicated in the pathogenesis of a number of renal diseases, such as urolithiasis. Protein function: [Alpha-1-microglobulin]: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments (PubMed:11877257, PubMed:15683711, PubMed:22096585, PubMed:23157686, PubMed:23642167, PubMed:25698971, PubMed:32823731, PubMed:32092412). Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis (PubMed:11877257, PubMed:32092412). Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential (PubMed:15683711). Upon acute inflammation, inhibits oxidation of low- density lipoprotein particles by MPO and limits vascular damage (PubMed:25698971). Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures (PubMed:23642167, PubMed:22096585). Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation (PubMed:21356557). Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria (PubMed:23157686, PubMed:32823731). Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (PubMed:15683711). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment. [The UniProt Consortium]