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Sigma-Aldrich

Albumin, Bovine Serum, Fraction V, Modified Cohn, pH 5.2

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Synonym(s):
Albumin, Bovine Serum, Fraction V, Modified Cohn, pH 5.2
CAS Number:
9048-46-8

Assay

≥96% (SDS-PAGE)

form

solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze

impurities

≤5% Moisture

color

off-white

solubility

0.15 M sodium chloride: 10 mg/mL

cation traces

heavy metals: ≤50 ppm

shipped in

ambient

storage temp.

2-8°C

Related Categories

General description

Albumin, Bovine Serum, Fraction V, Modified Cohn, pH 5.2 is a native fatty acid profile that reflects endogenous lipids. It has a pH in the range of 4.8-5.4 in 150 mM NaCl (1%).
Bovine serum albumin (BSA), a non-glycosylated globular, α-helical protein, belongs to the serum albumin family. It consists of three domains with two sub-domains each and has 17-disulfide bonds.

Application

Albumin, Bovine Serum, Fraction V, Modified Cohn, pH 5.2 has been used as a blocking agent in western blotting. It has also been used as a component in phosphate-buffered saline (PBS) for diluting secondary antibodies and blocking in immunofluorescence to observe the localization of the Golgi apparatus.

Biochem/physiol Actions

Bovine Serum Albumin (BSA) is the most vital component of cell culture media. It aids in the differentiation of embryonic stem cells (hESC). It plays a key role in the transportation of drugs, hormones, and fatty acids. BSA is used in enzyme-linked immunosorbent assay (ELISA) as a blocking agent.

Warning

Toxicity: Standard Handling (A)

Reconstitution

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Anna Eslami et al.
Journal of visualized experiments : JoVE, (44) (2010-12-30)
Western blotting is an analytical technique used to detect specific proteins in a given sample of tissue homogenate or extract. It uses gel electrophoresis to separate native or denatured proteins by the length of the polypeptide (denaturing conditions) or by
Miyu Tsuchiya et al.
Oncology letters, 11(5), 3279-3286 (2016-04-29)
N-glycosylation is a post-translational protein modification with a wide variety of functions. It has been predicted that R-spondin1 (RSPO1) is N-glycosylated, although this remains unknown. The present study identified that RSPO1 was N-glycosylated at Asn137, and that N-glycosylation of RSPO1
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
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