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The Anti-HSA Protein A Scaffold molecule binds with high affinity to native albumin from human, mouse and rat serum. The Anti-HSA Protein A Scaffold molecule can be used as capture reagent or detection reagent in ELISA. It is also well suited for affinity chromatography and depletion of HSA from human serum. The Anti-HSA Protein A Scaffold molecule is modified with a unique C-terminal cysteine for directed single-point chemical modification, facilitating labeling with fluorescent dyes, biotin or coupling to matrices.
ELISA, Affinity chromatography.
Anti-HSA Protein A scaffold molecule binds to native human serum albumin (HSA) and also to serum albumin of mouse and rat origin.
At +4°C is recommended for lyophilized protein. For reconstituted protein in physiological buffer, short-term storage at +4°C is recommended. For long-term storage, the protein solution should be aliquoted and then stored at -20°C. There is no decrease in
Human serum albumin (HSA), a soluble, monomeric protein, is the most abundant protein in human serum. Normal levels are 40-60 mg/ml HSA in blood; however the amount of HSA decreases upon infection. HSA acts primarily as a carrier protein for steroids, fatty acids and thyroid hormones, and it stabilizes extracellular fluid volume. Serum albumin is produced by the liver as pre-proalbumin and it is cleaved twice before secretion.
Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.