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A4737

Sigma-Aldrich

Bovine Serum Albumin

lyophilized powder, protease, essentially free, ≥98% (agarose gel electrophoresis)

Synonym(s):

Albumin from bovine serum, Albumin bovine serum, BSA, Bovine albumin

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About This Item

CAS Number:
9048-46-8
EC Number:
232-936-2
MDL number:
MFCD00130384
UNSPSC Code:
12352202

biological source

bovine

Assay

≥98% (agarose gel electrophoresis)

form

lyophilized powder

mol wt

~66 kDa

packaging

poly bottle of

origin

New Zealand origin

technique(s)

ligand binding assay: suitable

impurities

≤8.0% water (Karl Fischer)

pH

4.8-7.5

solubility

H2O: soluble 50 mg/mL

UniProt accession no.

P02769

foreign activity

protease, essentially free

storage temp.

2-8°C

Gene Information

bovine ... ALB(280717)

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General description

The most abundant plasma protein in mammals is albumin. It is produced in the liver and transferred as a non-glycosylated protein into the plasma. This multifunctional protein can bind to ligands.

Application

Bovine serum albumin (BSA) is extensively used for drug delivery since it is widely available, cheap and easily purified, has ligand-binding properties, and is widely accepted in the pharmaceutical industry.

Biochem/physiol Actions

Albumin is the most important circulatory protein involved in the control of Ca2+ (and Mg2+) levels in mammals.
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.

Preparation Note

Purified by chromatography
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.
Sourced and manufactured in New Zealand

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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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Ting Gong et al.
Biology of reproduction, 95(6), 116-116 (2016-09-30)
Saccharin sodium consumption is considered safe and beneficial, owing to its very intense sweetness without any associated calories, but supporting scientific data remain sparse and controversial. Herein, we demonstrate that dose-response relationships existed with regard to administration of saccharin or
Yuangang Zu et al.
International journal of nanomedicine, 8, 1207-1222 (2013-04-10)
The livertaxis of glycyrrhizic acid-conjugated bovine serum albumin (GL-BSA) has been reported in the literature. Now, in this paper, we describe a novel type of drug-targeted delivery system containing 10-hydroxycamptothecin (HCPT) with liver tumor targeting. First, GL was coupled to
Karolina A Majorek et al.
Molecular immunology, 52(3-4), 174-182 (2012-06-09)
Serum albumin (SA) is the most abundant plasma protein in mammals. SA is a multifunctional protein with extraordinary ligand binding capacity, making it a transporter molecule for a diverse range of metabolites, drugs, nutrients, metals and other molecules. Due to
Junaid Akhtar et al.
Bio-protocol, 10(4), e3520-e3520 (2021-03-04)
Chromatin immunoprecipitation is extensively used to investigate the epigenetic profile and transcription factor binding sites in the genome. However, when the starting material is limited, the conventional ChIP-Seq approach cannot be implemented. This protocol describes a method that can be
Ignacio Izeddin et al.
PloS one, 6(1), e15611-e15611 (2011-01-26)
The actin cytoskeleton of dendritic spines plays a key role in morphological aspects of synaptic plasticity. The detailed analysis of the spine structure and dynamics in live neurons, however, has been hampered by the diffraction-limited resolution of conventional fluorescence microscopy.
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