The mouse monoclonal anti-human serum albumin antibody (mouse IgG2a isotype) is derived from the HSA-11 hybridoma, produced by the fusion of mouse myeloma cells and BALB / c mouse splenocytes immunized with human serum albumin ( HSA). Monoclonal anti-human serum albumin specifically recognizes human albumin derived from serum, plasma, or liver cells. HSA is encoded by the gene mapped to human chromosome 4q13.3. It is characterized by three homologous domains that assemble to form a heart-shaped molecule.
HSA constitutes about 60-65% of total serum protein. The human serum albumin (HSA) gene is located on human chromosome 4. It encodes a globular protein that is the most prominent protein in human serum. It reaches a total concentration of approximately 60% of the total proteins in the blood serum. The globular protein is made up of 585 amino acids and consists of three globular domains that resemble each other in structure, each of which contains two subdomains.
The anti-human serum albumin antibody recognizes human albumin derived from serum, plasma, or liver cells.
Human serum albumin
The antibody can be used in an enzyme-linked immunosorbent assay (ELISA), immunoblotting (~ 70 kDa), and immunohistochemistry.
The solution in 0.01 M phosphate-buffered saline, pH 7.4, containing 15 mM sodium azide.
Storage and stability
For continuous use, store at 2-8 ° C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing are not recommended. If slight cloudiness occurs after prolonged storage, rinse the solution by centrifugation before use. Dilution working samples should be discarded if not used within 12 hours.
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Biochemical / Physiological Actions
Human serum albumin (HAS) serves as a transport and depot protein for various endogenous ligands including fatty acids, hormones, steroids, bilirubin, and heme. The high intravascular concentration of HSA allows it to play an essential role in exerting colloid osmotic pressure and thus regulating oncotic pressure and blood volume. It also acts as an antioxidant and is necessary to exert the Donnan effect on the capillaries. Mutations in the gene are associated with the development of bisalbuminemia or hypoalbuminemia.
Gene deficiency leads to analbuminemia. Human serum albumin (HSA) is a non-glycosylated single chain that has excellent binding capacity for various endogenous and exogenous ligands. It functions as a plasma transport molecule and is primarily bound to unesterified long-chain fatty acids. It also binds to and carries various metabolites, such as bilirubin, steroid hormones, thyroxine, tryptophan, certain vitamins, and metal ions within the body.
It also has the ability to bind to various drugs and affects their pharmacokinetics and pharmacodynamics. HSA functions as a carrier for NO and is also responsible for the antioxidant capacity of human serum. In acute hemolysis, SAH binds to heme in the bloodstream and is transported to hemopexin, where it is reabsorbed by parenchymal cells in the liver.