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Merck

126626

Bovine Serum Albumin

30% Sterile-Filtered Aqueous Solution, Preservative-Free

Synonyme(s) :

Albumin, Bovine Serum, 30% Sterile-Filtered Aqueous Solution, Preservative-Free

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About This Item

Numéro CAS:
9048-46-8
MDL number:
MFCD00130384
UNSPSC Code:
12352202
NACRES:
NA.25

Nom du produit

Albumin, Bovine Serum, 30% Sterile-Filtered Aqueous Solution, Preservative-Free,

form

liquid

description

Merck USA index - 14, 8468

assay

≥96% (agarose gel electrophoresis)

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze

technique(s)

immunohistochemistry: suitable

color

pale amber

shipped in

ambient

storage temp.

2-8°C

Quality Level

100

Catégories apparentées

Application

Albumin, Bovine Serum, 30% Sterile-Filtered Aqueous Solution, Preservative-Free has been used as a component of fluorescence-activated cell sorting (FACS) buffer to obtain a HaloTag CRISPR clone using FACS.

Biochem/physiol Actions

Bovine Serum Albumin (BSA) is a critical component of cell culture media. It is useful for embryonic stem cells (hESC) differentiation and helps to transport drugs, hormones, and fatty acids. BSA works as a blocking agent in enzyme-linked immunosorbent assay (ELISA).

Disclaimer

Toxicity: Standard Handling (A)

General description

Albumin, Bovine Serum, 30% Sterile-Filtered Aqueous Solution, Preservative-Free is used as a stabilizing agent and carrier protein.
Bovine serum albumin (BSA) is an α-helical, non-glycosylated globular protein with 17-disulfide bonds. It is a member of the serum albumin family and has three domains with two sub-domains each.

Physical form

Supplied as a 30% sterile-filtered solution in water, preservative-free.

Legal Information

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

Classe de stockage

10 - Combustible liquids

wgk

WGK 3

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Consulter la Bibliothèque de documents

Elizabeth A Caine et al.
Current protocols in pharmacology, 91(1), e81-e81 (2020-12-18)
To assess the role of a protein, protein loss phenotypic studies can be used, most commonly through mutagenesis RNAi or CRISPR knockout. Such studies have been critical for the understanding of protein function and the identification of putative therapeutic targets
Casey A Thornton et al.
Nature communications, 12(1), 1274-1274 (2021-02-26)
High-throughput single-cell epigenomic assays can resolve cell type heterogeneity in complex tissues, however, spatial orientation is lost. Here, we present single-cell combinatorial indexing on Microbiopsies Assigned to Positions for the Assay for Transposase Accessible Chromatin, or sciMAP-ATAC, as a method
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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