A7888
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:
UNSPSC Code:
12352202
EC Number:
232-936-2
NACRES:
NA.27
MDL number:
eCl@ss:
32160409
Biological source:
bovine
Assay:
≥96%
Form:
lyophilized powder
Technique(s):
blood typing: suitable
Impurities:
BT and VSV virus, tested
biological source
bovine
assay
≥96%
form
lyophilized powder
quality
suitable for RIA
Quality Level
Gene Information
bovine ... ALB(280717)
purified by
heat shock fractionation
packaging
poly bottle of
origin
USA origin
technique(s)
blood typing: suitable
impurities
BT and VSV virus, tested
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
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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)
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.
Disclaimer
May yield an insulin blank of up to 0.1 μunit per mg in certain procedures.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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
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
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
Sampada Chande et al.
Scientific reports, 10(1), 3069-3069 (2020-02-23)
Low blood phosphate (Pi) reduces muscle function in hypophosphatemic disorders. Which Pi transporters are required and whether hormonal changes due to hypophosphatemia contribute to muscle function is unknown. To address these questions we generated a series of conditional knockout mice
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)
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