Description: Purified native Mouse Albumin protein

Description: Recombinant Serum amyloid A protein

Description: Lyophilized Human Serum Albumin (>96% pure)

Description: Cell culture grade recombinant Human Serum Albumin protein

Description: Human serum albumin (HSA), the most abundant protein in human blood plasma, is essential for maintaining osmotic pressure. It is produced in the liver, consists of a single polypeptide chain, with 585 amino acids with 17 tyrosil residues and one tryptophan located in position 214. HSA is organized in three domains, I, II and III, each consisting of two subdomains, A and B. In the physiological states, HSA occurs in two forms – the non-modified HSA with a free thiol group of Cys-34, and the modified (oxidized) form (oHSA), also called human mercaptoalbumin (HMA) and human nonmercaptoalbumin (HNA), respectively. HMA and HNA are in equilibrium, depending on the redox state of Cys-34, and their ratio also varies depending on age and the diseased state. HSA functions primarily as a carrier protein for drugs, steroids, fatty acids, and thyroid hormones, and plays a role in stabilizing extracellular fluid volume.

Description: Human serum albumin (HSA) is also known as ALB,which is the main protein of plasma and has a good binding capacity for water,Ca2+,Na+,K+,fatty acids,hormones, bilirubin and drugs.The main function of HSA is the regulation of the colloidal osmotic pressure of blood. As Major zinc transporter in plasma, HSA typically binds about 80% of all plasma zinc.A variant structure of albumin could lead to increased binding of zinc resulting in an asymptomatic augmentation of zinc concentration in the blood. Defects in serum albumin can cause familial dysalbuminemic hyperthyroxinemia which is a form of euthyroid hyperthyroxinemia that is due to increased affinity of serum albumin for T4.It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.