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Safety Information

A9430

Sigma-Aldrich

Bovine Serum Albumin

heat shock fraction, low endotoxin, pH 7, ≥98%

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Synonym(s):
Albumin bovine serum, BSA, Bovine albumin
CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.27

biological source

bovine

Quality Level

Assay

≥98%

form

lyophilized powder

mol wt

~66 kDa

purified by

heat shock fractionation

packaging

poly bottle of

origin

USA origin

technique(s)

ELISA: suitable
microbiological culture: suitable

impurities

≤1.0 EU/mg endotoxin

loss

≤5%

pH

7

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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Application

This A9430 BSA product has been used in various systems and studies, including:
  • HK-2 cells: Ishola, D.A., Jr. et al., Kidney International, 70, 724-731 (2006).
  • Mice:
For vasoconstriction studies: Szczepaniak, W.S. et al., Am. J. Physiol. Lung Cell. Mol. Physiol., 299(1), L137-L145 (2010)
For studies of protein overload nephropathy:
a) Chang, A.M. et al., Nephrol. Dial. Transplant., 27, 1330-1343 (2012)
b) Wong, D.W.L. et al., Cell Death Dis., 7, e2155 (2016).
For protein overload related to resistance to loop diuretics: Zhuang, Y., Jia, Z., et al., Oncotarget, 8(44), 75808-75821 (2017).

Biochem/physiol Actions

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

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.

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Brittney M Rush et al.
Kidney international, 99(1), 102-116 (2020-08-21)
The nuclear factor erythroid 2-related factor 2 (Nrf2) pathway upregulates key cellular defenses. Clinical trials are utilizing pharmacologic Nrf2 inducers such as bardoxolone methyl to treat chronic kidney disease, but Nrf2 activation has been linked to a paradoxical increase in
Alexandria J Hammond et al.
PLoS pathogens, 17(4), e1009158-e1009158 (2021-04-06)
Binding of Streptococcus pneumoniae (Spn) to nasal mucus leads to entrapment and clearance via mucociliary activity during colonization. To identify Spn factors allowing for evasion of mucus binding, we used a solid-phase adherence assay with immobilized mucus of human and
Björn Hartleben et al.
PloS one, 7(5), e36705-e36705 (2012-05-16)
The kidney filter represents a unique assembly of podocyte epithelial cells that tightly enwrap the glomerular capillaries with their complex foot process network. While deficiency of the polarity proteins Crumbs and aPKC result in impaired podocyte foot process architecture, the
Marcos V A S Navarro et al.
PLoS biology, 9(2), e1000588-e1000588 (2011-02-10)
The bacterial second messenger bis-(3'-5') cyclic dimeric guanosine monophosphate (c-di-GMP) has emerged as a central regulator for biofilm formation. Increased cellular c-di-GMP levels lead to stable cell attachment, which in Pseudomonas fluorescens requires the transmembrane receptor LapD. LapD exhibits a
Tânia Veiga et al.
Eukaryotic cell, 11(2), 238-249 (2011-12-14)
The industrial production of penicillin G by Penicillium chrysogenum requires the supplementation of the growth medium with the side chain precursor phenylacetate. The growth of P. chrysogenum with phenylalanine as the sole nitrogen source resulted in the extracellular production of

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