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Anti-BSA Polyclonal Antibody

based on 1 citations in multiple journalsAnti-BSA Polyclonal Antibody14.1 4
Catalog #: 5998
SKU-Size Size Price Qty
5998-30T 30 µg
5998-100 100 µg
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Product Details

Antibody Target BSA
Alternate Name BSA Polyclonal Antibody, Anti-BSA Polyclonal antibody, BSA antibody, Anti-BSA, BSA, bovine serum albumin, AGE-BSA
Host Rabbit
Antibody Type Polyclonal
Isotype Rabbit IgG
Immunogen AGE-BSA
Accession # NP_851335
Gene ID 280717
Appearance Colorless liquid
Formulation 0.5 mg/ml affinity purified rabbit polyclonal antibody in phosphate buffered saline (PBS), pH 7.2, containing 30% glycerol, 0.5 mM EDTA, and 0.03% Proclin.
Purification Affinity purified
Species Reactivity Bovine
Application Western blot
Application & Usage Western blotting to detect BSA and AGE-BSA. We recommend using 1 µg/ml dilution. However, the optimal conditions should be determined individually.
Handling The antibody solution should be gently mixed before use.
Storage Conditions -20 °C
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not For Use in Humans.


Bovine serum albumin (BSA) is an abundant plasma protein in cows that is important for maintaining osmotic pressure in blood plasma for proper distribution of body fluids between intravascular compartments and body tissues. BSA is a common buffer component for immunoglobulin type assays due to good solubility characteristics for water, Ca2+, Na+, K+, fatty acids, hormones and bilirubin. BSA makes up about half of the protein in plasma and represents the most stable and soluble protein in the plasma. It is a suitable reagent for laboratories developing immunoassays, mostly due to its availability, solubility and the numerous functional groups present for coupling. The BSA component contains several lysines that are capable of reacting with conjugation sites of linkers, making it applicable as a carrier protein for antigenic compounds.

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Masayuki Amano, Amino-acid inserts of HIV-1 capsid (CA) induce CA degradation and abrogate viral infectivity: Insights for the dynamics and mechanisms of HIV-1 CA decomposition. Sci Rep., July 2019; 31285456.
Murali NS et al. (2007) Am J. Physiol. Renal Physiol. 292: F837- F844.
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