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A7888

Sigma-Aldrich

Bovine Serum Albumin

heat shock fraction, suitable for RIA, 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

grade

RIA grade

Assay

≥96%

form

lyophilized powder

quality

suitable for RIA

mol wt

~66 kDa

purified by

heat shock fractionation

packaging

poly bottle of

origin

USA origin

technique(s)

blood typing: suitable

loss

≤5%

pH

5.2

solubility

water: soluble (40 mg/ml)

suitability

suitable for insulin RIA procedures

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 (BSA) is 66 kDa protein consisting of three domains with two subdomains under each. It is α-helical globular and a non-glycosylated protein.

Application

Bovine Serum Albumin has been used:
  • as a blocking agent in enzyme linked immunosorbent assay (ELISA)(154)
  • as a component of Dulbecco PBS medium for preantral follicles culture(155)
  • as a component of modified Tris-buffered medium (mTBM) for oocyte insemination(156)

Biochem/physiol Actions

Bovine Serum Albumin (BSA) is a transporter for drugs, hormones and fatty acids. It is a blocking agent used in enzyme linked immunosorbent assay (ELISA) for preventing non-specific binding of antigens and antibodies to the microtiter plates. The cysteine and tyrosine residues of BSA have high affinity for metal binding.
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.

Features and Benefits

  • Heat shock fractionated
  • Suitable for radioimmunoassay (RIA)

Caution

May yield an insulin blank of up to 0.1 μunit per mg in certain procedures.

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 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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Lara Vlietstra et al.
PloS one, 14(6), e0217462-e0217462 (2019-06-07)
To determine if there is an association between sarcopenia, physical function and self-reported fatigue in osteoarthritis (OA) and rheumatoid arthritis (RA). A cross-sectional analysis of measurements from a cohort of 157 participants with OA or RA was performed. The relationship
K B Cullberg et al.
Nutrition & diabetes, 4, e113-e113 (2014-03-26)
High levels of free fatty acids (FFA) have been suggested to be one of the underlying mechanisms for adipose tissue (AT) inflammation and dysfunction in obesity. Human AT produces several adipokines including monocyte chemoattractant protein-1 (MCP-1), which are involved in
Enzyme-linked immunosorbent assay (ELISA) and blocking with bovine serum albumin (BSA)?not all BSAs are alike
Xiao Y and Isaacs SN
Journal of Immunological Methods, 384(1-2), 148-151 (2012)
Yankel Chekli et al.
Scientific reports, 10(1), 15791-15791 (2020-09-27)
Bacterial proteins exported to the cell surface play key cellular functions. However, despite the interest to study the localisation of surface proteins such as adhesins, transporters or hydrolases, monitoring their dynamics in live imaging remains challenging, due to the limited
Bovine serum albumin interactions with metal complexes
Topalua T, et al.
Clujul Medical (1957), 87(4), 215-215 (2014)

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