V900933
Bovine Serum Albumin
≥98%, ≤5% Loss on drying, suitable for western blot
Synonym(s):
Bovine Serum Albumin, Albumin bovine serum, BSA, Bovine albumin
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About This Item
grade
reagent grade
Quality Level
product line
Vetec™
Assay
≥98%
form
lyophilized powder
mol wt
~66 kDa
~66 kDa
technique(s)
western blot: suitable
impurities
≤5% Loss on drying
storage temp.
2-8°C
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General description
Bovine serum albumin (BSA) is a 66.4kDa, water-soluble protein. It has a single polypeptide chain consisting of about 583 amino acid residues and no carbohydrates. BSA possesses three homologous domains formed by six a-helices. Depending on pH, it undergoes reversible conformational isomerization. The native structure of the protein becomes reactive and flexible on heating.
Application
Bovine serum albumin (BSA) has been used:
- as a standard in Bradford protein assay method for protein quantification
- to study the formation of multiligand complex of BSA with retinol, resveratrol and (-)-epigallocatechin-3-gallate (EGCG)
- to study the adsorption of BSA by biochar (charcoal produced from plant matter)
Biochem/physiol Actions
Bovine serum albumin (BSA) has been used as a model protein in various studies, such as immunodiagnostic procedures, cell culture media and clinical chemistry.
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.
Legal Information
Vetec is a trademark of Merck KGaA, Darmstadt, Germany
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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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Xiaojun Ding et al.
Oncology letters, 13(4), 2281-2289 (2017-04-30)
Krüppel-like factor 7 (KLF7) is a member of the KLF family of zinc finger transcription factors, and was the first KLF cloned using complementary DNA and polymerase chain reaction (PCR) techniques with human vascular endothelial cells as a template. In
Formation of a Multiligand Complex of Bovine Serum Albumin with Retinol, Resveratrol, and (-)-Epigallocatechin-3-gallate for the Protection of Bioactive Components.
Wu Y, et al.
Journal of Agricultural and Food Chemistry, 65(14), 3019-3030 (2017)
Frank W P
The Plasma Proteins: Structure, Function, and Genetic Control, 1, 141-141 (1975)
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, 12210-12210 (2015)
Kinetics of thermal denaturation and aggregation of bovine serum albumin.
Borzova V A, et al.
PLoS ONE, 11(4), e0153495-e0153495 (2016)
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