A0281
Bovine Serum Albumin
lyophilized powder, essentially fatty acid free and essentially globulin free, ≥99% (agarose gel electrophoresis)
Synonym(s):
Albumin bovine serum, BSA, Bovine albumin
Sign Into View Organizational & Contract Pricing
All Photos(7)
About This Item
Recommended Products
biological source
bovine
Quality Level
Assay
≥99% (agarose gel electrophoresis)
form
lyophilized powder
mol wt
~66 kDa
purified by
cold ethanol and heatshock fractionation
packaging
poly bottle of
origin
USA origin
free fatty acid content
≤0.01%
technique(s)
enzyme immunoassay: suitable
impurities
essentially globulin free
≤0.01% Fatty acids
pH
7
solubility
water: soluble (40 mg/ml)
UniProt accession no.
storage temp.
2-8°C
Gene Information
bovine ... ALB(280717)
Looking for similar products? Visit Product Comparison Guide
General description
Bovine serum albumin (BSA) is a plasma protein with a calculated molecular weight (MW) of 66,430 Daltons (Da). The major protein in bovine serum, BSA assists in regulation of blood colloidal osmotic pressure. BSA is used in different applications such as immunochemistry, protein quantitation, and cell culture.
This BSA product is specifically tested for the following properties:
This BSA product is specifically tested for the following properties:
- very low FA content / essentially fatty acid free
- low globulin content / essentially globulin free
Application
BSA is a known fatty acid (FA) carrier. Thus when BSA is used specifically in cell culture, control over specific FA′s used to culture cell lines is important, because different cell lines can be variably sensitive to particular fatty acids. Fatty acid-free BSA thus is useful for cell culture work, where the specific FA content must be stringently controlled, so that researchers can control the specific fatty acids needed for their particular cell lines. Fatty acid-free albumin also allows for optimal and maximum binding sites for the specific fatty acids that researchers wish to use in their particular cell culture experiments. Use of FA-free BSA also addresses concerns about endogenous FA′s potentially in non-FA-free BSA.
Biochem/physiol Actions
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.
Features and Benefits
- Essentially fatty acid-free
- Essentially globulin-free
Preparation Note
Purified by a combination of heat shock and ethanol 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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
Viviana I Risca et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(8), 2913-2918 (2012-02-07)
Mechanical cues affect many important biological processes in metazoan cells, such as migration, proliferation, and differentiation. Such cues are thought to be detected by specialized mechanosensing molecules linked to the cytoskeleton, an intracellular network of protein filaments that provide mechanical
Bidur Paudel et al.
Biology of reproduction, 100(2), 440-454 (2018-09-22)
Mammalian sperm undergo a series of biochemical and physiological changes collectively known as capacitation in order to acquire the ability to fertilize. Although the increase in phosphorylation associated with mouse sperm capacitation is well established, the identity of the proteins
Noriko Kondo-Okamoto et al.
Molecular biology of the cell, 17(9), 3756-3767 (2006-06-23)
Although it is clear that mitochondrial morphogenesis is a complex process involving multiple proteins in eukaryotic cells, little is known about regulatory molecules that modulate mitochondrial network formation. Here, we report the identification of a new yeast mitochondrial morphology gene
Stephanie Moore et al.
Journal of chromatography. A, 1476, 1-8 (2016-11-24)
Despite the developments for faster liquid chromatographic and mass spectral detection techniques, the standard in-solution protein digestion for proteomic analyses has remained relatively unchanged. The typical in-solution trypsin protein digestion is usually the slowest part of the workflow, albeit one
Niina Aaltonen et al.
Biological procedures online, 22, 6-6 (2020-03-20)
Serine hydrolases (SHs) are a functionally diverse family of enzymes playing pivotal roles in health and disease and have emerged as important therapeutic targets in many clinical conditions. Activity-based protein profiling (ABPP) using fluorophosphonate (FP) probes has been a powerful
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service