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A9418

Sigma-Aldrich

Bovine Serum Albumin

lyophilized powder, BioReagent, suitable for cell culture

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.75

biological source

bovine

Quality Level

product line

BioReagent

Assay

≥96% (agarose gel electrophoresis)

form

lyophilized powder

mol wt

~66 kDa

origin

USA origin

technique(s)

cell culture | mammalian: suitable

loss

≤5%

pH

5.0-5.6

solubility

H2O: 40 mg/mL

foreign activity

BT virus, none detected
VSV virus, none detected

shipped in

ambient

storage temp.

2-8°C

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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 the washing solution for flow cytometry analysis, tissue digestion solution and blocking solution for ELISA (enzyme-linked immunosorbent assay). It has also been used in the resuspension buffer for flow cytometry.

Biochem/physiol Actions

Bovine serum albumin is broadly used as an additive to cell culture media, especially serum-free media. It provides a range of benefits including protection from oxidative damage and stabilization of other media components such as fatty acids and pyridoxal.
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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Intercellular adhesion molecule-1/LFA-1 cross talk is a proximate mediator capable of disrupting immune integration and tolerance mechanism at the feto-maternal interface in murine pregnancies.
Blois S et al.
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There is no effective treatment for autoimmune biliary diseases. Therefore, understanding their immunopathology is crucial. The biliary epithelial cells (BEC), expressing TLR-4, are constantly exposed to gut microbes and bacterial wall LPS, and in settings of inflammation, the immune infiltrate
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 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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