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A5611

Sigma-Aldrich

Bovine Serum Albumin

Cohn Fraction V, lyophilized powder, ≥96% (agarose gel electrophoresis)

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Synonym(s):
Albumin bovine serum, BSA, Bovine albumin
CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.25

biological source

bovine

Quality Level

Assay

≥96% (agarose gel electrophoresis)

form

lyophilized powder

mol wt

~66 kDa

packaging

poly bottle of

origin

USA origin

technique(s)

immunohistochemistry: suitable

pH

4.8-7.5

solubility

H2O: soluble 40 mg/mL, clear to slightly hazy, yellow

UniProt accession no.

storage temp.

2-8°C

Gene Information

bovine ... ALB(280717)

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General description

Serum albumins are soluble constituents of the circulatory system. Bovine serum albumin (BSA) is homologous to human serum albumin (HSA). BSA consists of three homologous domains (I, II, III), that are separated into nine loops by disulfide bonds. Serum albumin acts as a depot protein.

Application

Bovine Serum Albumin has been used:
  • for in vitro high molecular weight (HMW)-species formation assay
  • for immunohistochemistry
  • in Escherichia coli quantitative polymerase chain reaction (qPCR) analysis

Biochem/physiol Actions

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.
This is a cold alcohol fractionated albumin that is produced by Sigma-Aldrich with a stricter adherence to the original Cohn method of fractionation than other commercially available bovine albumins.

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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S Valera et al.
Proceedings of the National Academy of Sciences of the United States of America, 89(20), 9949-9953 (1992-10-15)
The major brain nicotinic acetylcholine receptor is assembled from two subunits termed alpha 4 and n alpha 1. When expressed in Xenopus oocytes, these subunits reconstitute a functional acetylcholine receptor that is inhibited by progesterone levels similar to those found
Standardized data quality acceptance criteria for a rapid Escherichia coli qPCR method (Draft Method C) for water quality monitoring at recreational beaches
Sivaganesan M, et al.
Water Research (2019)
X Sui et al.
Proceedings of the National Academy of Sciences of the United States of America, 92(7), 2859-2863 (1995-03-28)
gp130, a signal-transducing receptor component of interleukin 6 (IL-6), associates with an IL-6 and IL-6 receptor (IL-6) complex and transduces signals. To examine the role of gp130 signaling in the expansion of human hemopoietic progenitor cells, we tested the effects
Interaction of flavonoids with bovine serum albumin: a fluorescence quenching study
Papadopoulou A, et al.
Journal of Agricultural and Food Chemistry, 53(1), 158-163 (2005)
A A Spector et al.
Journal of lipid research, 10(1), 56-67 (1969-01-01)
We have studied the binding of long-chain free fatty acids (FFA) to crystalline bovine serum albumin (BSA) that had been extracted with charcoal to remove endogenous fatty acids. The data were analyzed in terms of a model consisting of six

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