126621
Bovine Serum Albumin
Cohn Fraction, 30% Aqueous Solution
Synonym(s):
Albumin, Bovine Serum, Cohn Fraction, 30% Aqueous Solution
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product name
Albumin, Bovine Serum, Cohn Fraction, 30% Aqueous Solution,
Assay
≥95% (agarose gel electrophoresis)
form
liquid
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
technique(s)
MALDI-TOF: suitable
shipped in
ambient
storage temp.
2-8°C
General description
Albumin, Bovine Serum, (BSA) Cohn Fraction is purified by cold ethanol precipitation (Cohn extraction) and by heat treatment to remove lipids and fatty acids. It is a single carbohydrate-free polypeptide and the most abundant (comprising ~60%) of the plasma proteins. BSA regulates the maintenance of osmotic pressure.
BSA belongs to the serum albumin family, comprising three domains with two sub-domains under each. BSA is an α-helical, globular, and non-glycosylated protein with 17-disulfide bonds.
Biochem/physiol Actions
Bovine serum albumin (BSA) transports sparingly soluble physiological substances, especially long-chain fatty acids, bilirubin, drugs, hormones, and fatty acids. It acts as a blocking agent in enzyme-linked immunosorbent assay (ELISA). BSA is a vital component of the cell culture media and boosts embryonic stem cells (hESC) differentiation.
Warning
Toxicity: Standard Handling (A)
Physical form
30% solution in 0.8% NaCl, 0.1% NaN₃, pH 7.2, sterile-filtered.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Certificates of Analysis (COA)
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Yuhong Xiao et al.
Journal of immunological methods, 384(1-2), 148-151 (2012-06-27)
The enzyme-linked immunosorbent assay (ELISA) is an extremely common and powerful laboratory technique for detecting proteins by antibodies. Researchers frequently use bovine serum albumin (BSA) as a blocking agent to prevent non-specific binding of antigens and antibodies to the microtiter
Geoffrey L Francis
Cytotechnology, 62(1), 1-16 (2010-04-08)
Albumin has a long historical involvement in design of media for the successful culture of mammalian cells, in both the research and commercial fields. The potential application of albumins, bovine or human serum albumin, for cell culture is a by-product
S Chodankar et al.
Physical review. E, Statistical, nonlinear, and soft matter physics, 77(3 Pt 1), 031901-031901 (2008-06-04)
Small-angle neutron scattering (SANS) and dynamic light scattering (DLS) have been used to study conformational changes in protein bovine serum albumin (BSA) due to perturbation in its native structure as induced by varying temperature and pressure, and in presence of
Tamara Topală et al.
Clujul medical (1957), 87(4), 215-219 (2014-01-01)
The continuous search for new molecules with therapeutic abilities has led to the synthesis and characterization of a large number of metal complexes, proven to exhibit potential as pharmacological agents through their antibacterial, antiviral, antifungal and antineoplastic properties. As serum
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