Skip to Content
MilliporeSigma
All Photos(1)

Key Documents

A7517

Sigma-Aldrich

Bovine Serum Albumin

For use as a marker in SDS-PAGE

Synonym(s):

Albumin bovine serum, BSA, Bovine albumin

Sign Into View Organizational & Contract Pricing


About This Item

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

biological source

bovine

Quality Level

assay

24-32 mg/vial (biuret)

form

lyophilized powder

mol wt

~66 kDa

purified by

cold ethanol fractionation

packaging

vial of 25 mg

origin

USA origin

technique(s)

electrophoresis: suitable

pH

5.2

solubility

water: slightly soluble

suitability

suitable for (Suitable for use as an electrophoresis marker)

UniProt accession no.

storage temp.

2-8°C

Gene Information

bovine ... ALB(280717)

Looking for similar products? Visit Product Comparison Guide

General description

Bovine Serum Albumin (BSA) is a globular and α-helical single-chain protein, produced in the liver. This non-glycosylated protein belongs to the serum albumins family. BSA consists of three homologous domains with two sub-domains each.

Application

Bovine Serum Albumin (BSA) has been used:
  • as a standard protein in the elution-filter aided proteome preparation (FASP) method and in sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE)
  • as a component of the molecular weight marker in SDS-PAGE and western blotting
  • as a blocking agent in immunofluorescence

Biochem/physiol Actions

Bovine Serum Albumin (BSA) participates in the transport of endogenous and exogenous substances, such as hormones, fatty acids, drugs, and xenobiotics. It is used as a blocking agent in enzyme-linked immunosorbent assay (ELISA). BSA is usually preferred for the preparation of serum-free media. It is used in the pharmaceutical and cosmetic industry.
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.

Preparation Note

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.

Recommended products

Discover LiChropur reagents ideal for HPLC or LC-MS analysis

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Feiran Hao et al.
The Analyst, 141(16), 4953-4960 (2016-06-17)
Currently, the separation targets of preparative electrophoresis range from milligrams to micrograms of proteins. However, most commercially available preparative electrophoretic instruments function at the milligram level. Although some preparative electrophoretic apparatuses operated at the microgram level, the fractionation results are
Mehdi Fazlalipour et al.
Jundishapur journal of microbiology, 8(4), e17157-e17157 (2015-06-03)
Gradual development of a useful vaccine can be the main point in the control and eradication of Hepatitis C virus (HCV) infection. Hepatitis C Virus envelope glycoproteins are considered as the main HCV vaccine candidate. In this study, the Pichia
Structural changes during the unfolding of Bovine serum albumin in the presence of urea: A small-angle neutron scattering study
Pramana, 63(2), 363-368 (2004)
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
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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service