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A4503

Sigma-Aldrich

Bovine Serum Albumin

cold ethanol fraction, pH 5.2, ≥96%

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

≥96%

form

lyophilized powder

mol wt

~66 kDa

purified by

cold ethanol fractionation

origin

USA origin

technique(s)

ELISA: suitable
blood typing: suitable
microbiological culture: suitable

loss

≤5%

pH

5.2

solubility

water: soluble (40 mg/ml)

UniProt accession no.

foreign activity

BT Virus, none detected
VSV Virus, none detected

storage temp.

2-8°C

Gene Information

bovine ... ALB(280717)

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General description

Bovine serum albumin is a model protein in various studies and is made up of 583 amino acids. It is a water-soluble protein with a molecular weight of 66.4kDa. Six α-helices form three homologous domains of BSA. Depending on pH, it undergoes reversible conformational isomerization. The native structure of the protein becomes reactive and flexible on heating.

Application

  • Bovine Serum Albumin has been used in solution prepared for the isolation of heart mitochondria.
  • It has been used in the cytotoxicity assay buffer.
  • It has been used for the induction of protein overload nephropathy in rats.

Biochem/physiol Actions

Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.

Preparation Note

Often referred to as Cohn fraction V; this product is prepared by a modified method of the Cohn cold ethanol fractionation method.
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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Cytochrome C effect on respiration of heart mitochondria: influence of various factors.
Toleikis A et al.
Bioscience Reports, 25, 387-387 (2005)
Rapamycin worsens renal function and intratubular cast formation in protein overload nephropathy.
Coombes JD et al.
Kidney International, 68, 2599-2599 (2005)
Sensitization of tumor cells to NK cell-mediated killing by proteasome inhibition.
Hallett WH et al.
Journal of Immunology, 180, 163-163 (2008)
Rui Zhang et al.
PLoS pathogens, 15(2), e1007329-e1007329 (2019-03-01)
Mycobacterial pathogens are the causative agents of chronic infectious diseases like tuberculosis and leprosy. Autophagy has recently emerged as an innate mechanism for defense against these intracellular pathogens. In vitro studies have shown that mycobacteria escaping from phagosomes into the
Isabella Marcomini et al.
Cell reports, 24(10), 2614-2628 (2018-09-06)
Multiple pathways regulate the repair of double-strand breaks (DSBs) to suppress potentially dangerous ectopic recombination. Both sequence and chromatin context are thought to influence pathway choice between non-homologous end-joining (NHEJ) and homology-driven recombination. To test the effect of repetitive sequences

Protocols

Spectrophotometric assay at 260 nm measures nuclease S1 activity, vital for nucleic acid research, with defined enzyme unit criteria.

Spectrophotometric assay at 260 nm measures nuclease S1 activity, vital for nucleic acid research, with defined enzyme unit criteria.

Spectrophotometric assay at 260 nm measures nuclease S1 activity, vital for nucleic acid research, with defined enzyme unit criteria.

Spectrophotometric assay at 260 nm measures nuclease S1 activity, vital for nucleic acid research, with defined enzyme unit criteria.

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