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A9647

Sigma-Aldrich

Bovine Serum Albumin

heat shock fraction, pH 7, ≥98%

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%

form

lyophilized powder

mol wt

~66 kDa

purified by

heat shock fractionation

origin

USA origin

technique(s)

immunocytochemistry: suitable

impurities

≤5.0% Loss on drying

loss

≤5%

pH

7

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 protein whose key biological function is to regulate the colloidal osmotic pressure of blood. BSA is widely used in various studies and applications. Made up of 583 amino acids, BSA is a water-soluble protein with a calculated molecular weight of 66,430 Da. 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 is used for many applications, including the following applications:
  • BSA has been used in cell culture, e.g. as a supplement in media prepared for culturing of oligodendrocytes.
  • BSA has been used for the dilution of primary antibody solution in immunohistochemistry procedures.
  • BSA has been used as a standard in the Bradford method of protein quantification.
  • BSA has been used in blocking and permeabilization buffer for immunofluorescence studies.

Biochem/physiol Actions

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

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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Mohammad Bahrami et al.
Scientific reports, 9(1), 11739-11739 (2019-08-15)
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Campos RS et al.
Urology, 67, 797-797 (2006)
Characterization of an Exo-beta-1,3-Glucanase Produced by Pichia anomala Strain K, Antagonist of Botrytis cinerea on Apples.
Jijakli MH et al.
Phytopathology, 88, 335-335 (1998)
Down-regulation of seladin-1 increases BACE1 levels and activity through enhanced GGA3 depletion during apoptosis.
Sarajarvi T et al.
The Journal of Biological Chemistry, 284, 34433-34433 (2009)
Corrigendum: Formation and reshuffling of disulfide bonds in bovine serum albumin demonstrated using tandem mass spectrometry with collision-induced and electron-transfer dissociation.
Rombouts I et al.
Scientific Reports, 5 (2015)

Articles

This solution is used as a substrate for detecting horseradish-peroxidase conjugates in Western blotting.

Silica monoliths with larger mesopores are a powerful tool for the fast separation of biomolecules including mAbs. The immobilization of protein A on epoxy-modified widepore (WP) silica rods enabled highly reproducible and fast, one minute, separations of mAbs. The Chromolith® WP 300 is also available with a protein A phase.

This page segues to comprehensive insights on how serum albumin and other important cell culture components affect the performance of serum-free cell culture systems used for biomanufacturing heterologous proteins including monoclonal antibodies. The page introduces the in vitro chemistry and biochemistry of albumin. These insights may also be applied to ex vivo and tissue engineering applications.

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