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A4919

Sigma-Aldrich

Bovine Serum Albumin

heat shock fraction, protease free, low endotoxin, suitable for cell culture, 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

Quality Level

product line

BioReagent

Assay

≥98%

form

lyophilized powder

mol wt

~66 kDa

purified by

heat shock fractionation

packaging

poly bottle of

origin

USA origin

technique(s)

cell culture | mammalian: suitable

impurities

protease, none detected
≤1.0 EU/mg endotoxin

loss

≤5%

pH

7

solubility

water: soluble (40 mg/ml)

UniProt accession no.

foreign activity

BT virus, none detected
Protease by FITC, 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), a 66 kDa protein, belongs to the family of serum albumins. It is an α-helical, non-glycosylated and globular protein, that has 17-disulfide bonds.

Application

Bovine Serum Albumin has been used:
  • as a component of cell culture media in cochlear explant culture
  • organotypic cultures and embryo culture
  • as a component of phosphate-buffered saline (PBS) in immunostaining of human induced pluripotent stem cell (hiPSC)

Biochem/physiol Actions

Bovine Serum Albumin (BSA) is the most vital constituent of the cell culture media, which aids embryonic stem cells (hESC) differentiation. It acts as a blocking agent in enzyme linked immunosorbent assay (ELISA) to inhibit non-specific binding of antigens and antibodies to the microtiter plates.
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.

Features and Benefits

  • Tested for use in cell culture
  • Protease-free
  • Low endotoxin

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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An immortalized microglial cell line (Mocha) derived from rat cochlea
Seigel GM, et al.
Molecular and Cellular Neurosciences, 85, 202-210 (2017)
Kanamycin damages early postnatal, but not adult spiral ganglion neurons
Gao K, et al.
Neurotoxicity Research, 32(4), 603-613 (2017)
Paternal breed effects on expression of IGF-II, BAK1 and BCL2-L1 in bovine preimplantation embryos
Valleh MV, et al.
Zygote, 23(5), 712-721 (2015)
Dalian Ding et al.
PloS one, 8(11), e79817-e79817 (2013-11-14)
Mefloquine is widely used for the treatment of malaria. However, this drug is known to induce neurological side effects including depression, anxiety, balance disorder, and sensorineural hearing loss. Yet, there is currently no treatment for these side effects. In this
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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