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126621

Sigma-Aldrich

Bovine Serum Albumin

Cohn Fraction, 30% Aqueous Solution

Synonym(s):

Albumin, Bovine Serum, Cohn Fraction, 30% Aqueous Solution

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About This Item

CAS Number:
UNSPSC Code:
12352202
NACRES:
NA.25

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

10 - Combustible liquids

wgk_germany

WGK 3


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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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