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A3912

Sigma-Aldrich

Bovine Serum Albumin

heat shock fraction, 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

Quality Level

Assay

≥96%

form

lyophilized powder

mol wt

~66 kDa

purified by

heat shock fractionation

packaging

poly bottle of

origin

USA origin

technique(s)

blood typing: suitable
microbiological culture: suitable

loss

≤5%

pH

5.2

solubility

water: soluble (40 mg/ml)

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 a 66.4 kDa, water-soluble protein composed of 583 amino acids. It has a single polypeptide chain with three homologous domains formed by six α-helices. Depending on pH, it undergoes reversible conformational isomerization. The native structure of the protein becomes reactive and flexible on heating. BSA has been used as a model protein in various applications, including immunodiagnostic procedures, cell culture media and clinical chemistry. Serum albumins facilitates drug disposition and efficacy by maintaining osmotic blood pressure.

Application

Bovine Serum Albumin (BSA) has been used:
  • to study its adsorption on a planar poly(acrylic acid) (PAA) brush layer through fixed-angle optical reflectometry
  • to measure its adsorption on a variety of thin films by means of total internal reflection spectroscopy
  • as a constituent of Krebs-Ringer bicarbonate buffer, which acts as a perfusate during placental perfusion

Biochem/physiol Actions

Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.

Quality

Remainder mostly globulins.

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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Adsorption of the protein bovine serum albumin in a planar poly (acrylic acid) brush layer as measured by optical reflectometry
de Vos WM, et al.
Langmuir, 24(13), 6575-6584 (2008)
Functional role of P-glycoprotein in the human blood-placental barrier
Molsa M, et al.
Clinical Pharmacology and Therapeutics, 78(2), 123-131 (2005)
Real-time analysis of protein adsorption to a variety of thin films
Sapsford KE and Ligler FS
Biosensors And Bioelectronics, 19(9), 1045-1055 (2004)
Yiwen Sun et al.
Biomedical optics express, 9(7), 2917-2929 (2018-07-10)
The development of new spectral analysis methods in bio thin-film detection has generated intense interest in terahertz (THz) spectroscopy and its application in a wide range of fields. In this paper, it is the first time that machine learning methods
Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin.
Hu Y J, et al.
Journal of Pharmaceutical and Biomedical Analysis, 36(4), 915-919 (2004)

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