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Merck

A3912

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:
UNSPSC Code:
12352202
EC Number:
232-936-2
NACRES:
NA.27
MDL number:

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Product Name

Bovine Serum Albumin, heat shock fraction, pH 5.2, ≥96%

biological source

bovine

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

impurities

BT and VSV virus, tested

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

Quality Level

Gene Information

bovine ... ALB(280717)

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This Item
A90562905-OPA7906
origin

USA origin

origin

USA origin

origin

-

origin

USA origin

biological source

bovine

biological source

bovine

biological source

-

biological source

bovine

technique(s)

blood typing: suitable, microbiological culture: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

-

technique(s)

blood typing: suitable, microbiological culture: suitable

assay

≥96%

assay

≥96% (agarose gel electrophoresis)

assay

≥99±% (electrophoresis)

assay

≥98%

Quality Level

200

Quality Level

200

Quality Level

100

Quality Level

300

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

Analysis Note

Remainder mostly globulins.

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[1]
  • to measure its adsorption on a variety of thin films by means of total internal reflection spectroscopy[2]
  • as a constituent of Krebs-Ringer bicarbonate buffer, which acts as a perfusate during placental perfusion[3]

Biochem/physiol Actions

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

General description

Bovine serum albumin (BSA) is a 66.4 kDa, water-soluble protein composed of 583 amino acids.[4][5] 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.[5] BSA has been used as a model protein in various applications, including immunodiagnostic procedures, cell culture media and clinical chemistry.[6] Serum albumins facilitates drug disposition and efficacy by maintaining osmotic blood pressure.[7]

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

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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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
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)
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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