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A6003

Sigma-Aldrich

Bovine Serum Albumin

lyophilized powder, essentially fatty acid free, ≥96% (agarose gel electrophoresis)

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.25

biological source

bovine

Quality Level

Assay

≥96% (agarose gel electrophoresis)
≥96%

form

lyophilized powder

mol wt

~66 kDa

purified by

cold ethanol fractionation

packaging

poly bottle of

origin

USA origin

free fatty acid content

≤0.01%

technique(s)

microbiological culture: suitable

impurities

≤0.01% fatty acid (GC)

pH

7

solubility

water: soluble (50 mg/ml)

UniProt accession no.

application(s)

hematology

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

BSA is a known carrier of fatty acids (FA). Thus control over the specific FA′s for culture of cell lines is important, as different cell lines can be differentially sensitive to particular fatty acids. Fatty acid-free BSA thus is a useful tool for cell culture experiments where the specific fatty acid content must be tightly controlled, to allow researchers to use particular fatty acids specific to their cell lines. Fatty acid-free albumin also allows for optimal and maximum binding sites for adding specific fatty acids to use in cell culture. The use of FA-free BSA also mitigates concerns about endogenous FA′s potentially in non-FA-free BSA.
Bovine serum albumin (BSA) is a highly abundant plasma protein that assists in the regulation of the colloidal osmotic pressure of blood. BSA is used in many different applications, such as cell culture, immunochemistry, and protein quantitation.

This BSA product is specifically tested for very low FA content / fatty acid free status.

Biochem/physiol Actions

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

Features and Benefits

  • Cold ethanol fractionated
  • Essentially fatty acid-free

Preparation Note

Often referred to as Cohn fraction V; this product is prepared by a modified method of the Cohn cold ethanol fractionation method.
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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Kevin Huynh et al.
Metabolites, 8(2) (2018-04-25)
Macrophages are abundant within adipose tissue depots where they are exposed to fatty acids, leading to lipid accumulation. Herein, we have determined the effects of various fatty acids on the macrophage lipidome. Using targeted mass-spectrometry, we were able to detect
Wendy W S Yue et al.
Proceedings of the National Academy of Sciences of the United States of America, 116(11), 5144-5153 (2019-02-24)
G protein-coupled receptor (GPCR) signaling is crucial for many physiological processes. A signature of such pathways is high amplification, a concept originating from retinal rod phototransduction, whereby one photoactivated rhodopsin molecule (Rho*) was long reported to activate several hundred transducins
Esmee Koedoot et al.
Nature communications, 10(1), 2983-2983 (2019-07-07)
Ttriple-negative breast cancer (TNBC) is an aggressive and highly metastatic breast cancer subtype. Enhanced TNBC cell motility is a prerequisite of TNBC cell dissemination. Here, we apply an imaging-based RNAi phenotypic cell migration screen using two highly motile TNBC cell
Ting Wang et al.
Journal of translational medicine, 13, 152-152 (2015-05-09)
Osteoinduction and proliferation of bone-marrow stromal cells (BMSCs) in three-dimensional (3D) poly(ε-caprolactone) (PCL) scaffolds have not been studied throughly and are technically challenging. This study aimed to optimize nanocomposites of 3D PCL scaffolds to provide superior adhesion, proliferation and differentiation
G I Lancaster et al.
Nature communications, 7, 10626-10626 (2016-02-04)
Protein kinase R (PKR) has previously been suggested to mediate many of the deleterious consequences of a high-fat diet (HFD). However, previous studies have observed substantial phenotypic variability when examining the metabolic consequences of PKR deletion. Accordingly, herein, we have

Protocols

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Enzymatic Assay of Neuraminidase applies to products that have a specification for neuraminidase content by enzymatic determination.

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Learn about bovine serum albumin (BSA) structure, molecular weight, function, solubility, how BSA is made, purification methods, applications and purchasing.

Learn about bovine serum albumin (BSA) structure, molecular weight, function, solubility, how BSA is made, purification methods, applications and purchasing.

Learn about bovine serum albumin (BSA) structure, molecular weight, function, solubility, how BSA is made, purification methods, applications and purchasing.

Learn about bovine serum albumin (BSA) structure, molecular weight, function, solubility, how BSA is made, purification methods, applications and purchasing.

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