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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A propos de cet article
Assay:
≥96% (agarose gel electrophoresis)
Form:
liquid
Technique(s):
immunohistochemistry: suitable
Service technique
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Laissez-nous vous aiderNom du produit
Albumin, Bovine Serum, 30% Sterile-Filtered Aqueous Solution, Preservative-Free,
description
Merck USA index - 14, 8468
Quality Level
assay
≥96% (agarose gel electrophoresis)
form
liquid
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
technique(s)
immunohistochemistry: suitable
color
pale amber
shipped in
ambient
storage temp.
2-8°C
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.
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).
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
Disclaimer
Toxicity: Standard Handling (A)
Classe de stockage
10 - Combustible liquids
wgk
WGK 3
Certificats d'analyse (COA)
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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans 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