A8022

Sigma-Aldrich

Bovine Serum Albumin

heat shock fraction, pH 5.2, ≥96%

Synonym(s):
Albumin bovine serum, Bovine albumin, BSA
CAS Number:
EC Number:
MDL number:
NACRES:
NA.27

Quality Level

biological source

bovine

assay

≥96%

form

lyophilized powder

mol wt

~66 kDa

purified by

heat shock fractionation

packaging

poly bottle of

origin

USA origin

application(s)

ELISA: suitable
electrophoresis: suitable
western blot: suitable

pH

5.2

solubility

water: soluble (40 mg/ml)

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 serum protein with a calculated molecular weight of 66,430 Daltons BSA consists of three domains with two subdomains under each, and is a α-helical, globular and non-glycosylated protein with 17-disulfide bonds.

BSA acts as a carrier protein for biomolecules like as fatty acids, amino acids, and steroids.

Application

Bovine Serum Albumin has been used:
  • with primary antibodies to prevent non-specific binding in immunohistochemistry of heart sections
  • as a component of trypsin inhibitor solution
  • as a component of sterile sorting buffer for immunocytochemistry of common lymphoid progenitor (CLP) cells

Although we have not specifically tested this product in the following applications, several publications have cited use of A8022 in various applications such as:
  • Embryo culture (Dobrinsky, J.R. et al., Biol. Reprod., 55(5), 1069-1074 (1996))
  • Oocyte culture medium (Jung, Y.J., and Cheon, Y.-P., Dev. Reprod., 18(2), 117-125 (2014))
  • Western blotting (Chronopoulos, A. et al., Nat. Commun., 7:7, 12630 (doi: 10.1038/ncomms12630) (2016)

Packaging

10, 50, 100, 500 g in poly bottle
1 kg in poly drum

Biochem/physiol Actions

Bovine Serum Albumin is used in many applications, such as the following:
  • A transporter for drugs, hormones and fatty acids.
  • As a blocking agent in enzyme linked immunosorbent assay (ELISA) for preventing non-specific binding of antigens and antibodies to microtiter plates
  • BSA is a crucial component of cell culture media and favors embryonic stem cells (hESC) differentiation.
  • BSA shares structural features with human serum albumin. Its high solubility, low cost and purity and interaction with surfactants make it useful in the cosmetic and pharmaceutical industries.
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.

Preparation Note

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.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

RIDADR

NONH for all modes of transport

WGK Germany

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

In vitro differentiation of murine innate lymphoid cells from common lymphoid progenitor cells
Seehus C and Kaye J
Bio-protocol, 6, 1770e-1770e (2016)
The sinus venosus myocardium contributes to the atrioventricular canal: potential role during atrioventricular node development?
Kelder TP, et al.
Journal of Cellular and Molecular Medicine, 19(6), 1375-1389 (2015)
Resistance of subventricular neural stem cells to chronic hypoxemia despite structural disorganization of the germinal center and impairment of neuronal and oligodendrocyte survival
de Tassigny XA, et al.
Hypoxia (Auckland, N.Z.), 3, 15-15 (2015)
A J Rice et al.
Oncogenesis, 6(7), e352-e352 (2017-07-04)
Increased matrix rigidity associated with the fibrotic reaction is documented to stimulate intracellular signalling pathways that promote cancer cell survival and tumour growth. Pancreatic cancer is one of the stiffest of all human solid carcinomas and is characterised by a...
Binding of fatty acid amide amphiphiles to bovine serum albumin: role of amide hydrogen bonding
Ghosh S and Dey J
The Journal of Physical Chemistry B, 119(25), 7804-7815 (2015)

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

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon

MilliporeSigma

Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.