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A3733

Sigma-Aldrich

Bovine Serum Albumin

lyophilized powder, ≥98% (agarose gel electrophoresis)

Synonym(s):

Albumin bovine serum, BSA, Bovine albumin

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.27

biological source

bovine

Assay

≥98% (agarose gel electrophoresis)

form

lyophilized powder

mol wt

~66 kDa

purified by

heat shock fractionation

packaging

poly bottle of

origin

New Zealand origin

technique(s)

flow cytometry: suitable

pH

7
~7 (1% in 0.15 M NaCl)

solubility

water: slightly soluble

UniProt accession no.

storage temp.

2-8°C

Gene Information

bovine ... ALB(280717)

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General description

Bovine serum albumin (BSA) that belongs to the serum albumin family, is an α-helical, globular and non-glycosylated protein. It comprises three domains with two subdomains under each domain.

Application

Bovine Serum Albumin has been used:
  • as a component of cryomedia for freezing testicular tissue
  • to resuspend myometrial cells in flow cytometric analysis for cell viability quantification
  • to block cardiac fibroblasts (CFs) for immunofluorescence staining

Biochem/physiol Actions

Bovine Serum Albumin (BSA) is a transporter for drugs, hormones, and fatty acids. It displays high solubility and is exploited in the cosmetic and pharmaceutical industries. BSA is useful as a cell media component and favors embryonic stem cells (hESC)differentiation.
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.

Preparation Note

Derived from New Zealand source serum
Prepared using heat shock fractionation
Serum albumin may be referred to as Fraction V. This naming convention is taken from the original Cohn method of fractionating serum proteins using cold ethanol precipitation. Serum albumin was found in the fifth ethanol fraction using Cohn′s method. Since then, the term "Fraction V" has been used by some to describe serum albumin regardless of the method of preparation. Others have used this term to describe serum albumin purified by ethanol fractionation methods that have been highly modified since the original Cohn method was described. Sigma-Aldrich manufactures and distributes serum albumins purified from a variety of primary methods including the true Cohn fractionation method, modified ethanol fractionation methods, heat shock and chromatography. Additional purification steps may include crystallization or charcoal filtration.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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Roman Franěk et al.
PloS one, 14(4), e0205481-e0205481 (2019-04-19)
Common carp (Cyprinus carpio) is one of the most cultured fish species over the world with many different breeds and plenty of published protocols for sperm cryopreservation. However, data regarding preservation of gonadal tissue and surrogate production is still missing.
Subhajit Ghosh et al.
The journal of physical chemistry. B, 119(25), 7804-7815 (2015-05-30)
The study of protein-surfactant interactions is important because of the widespread use of surfactants in industry, medicine, and pharmaceutical fields. Sodium N-lauroylsarcosinate (SL-Sar) is a widely used surfactant in cosmetics, shampoos. In this paper, we studied the interactions of bovine
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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