description
for research or for further manufacturing use
form
lyophilized powder
storage temp.
2-8°C
Application
Bovine serum albumin (BSA) makes up approximately 60% of all proteins in animal serum. It is commonly used in cell culture protocols, particularly when protein supplementation is necessary and the other components of serum are unwanted. In cell culture its main role is as a carrier of small molecules. Because of its negative charge, BSA binds water, salts, fatty acids, vitamins and hormones, then carries these bound components between tissues and cells. The binding capacity also makes BSA an effective scavenger for removing toxic substances, including pyrogens, from the medium. This product is prepared by removing the native lipids from the albumin. BSA-FAF often is used to deliver fatty acids and other lipids that are present in cell culture media.
Biochem/physiol Actions
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.
Preparation Note
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.
Regulatory Information
新产品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Related Content
Claus G Madsen et al.
European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V, 92, 1-7 (2015-02-11)
This study describes how protein release from polymer matrices correlate with simple measurements on the intrinsic viscosity of the polymer solutions used for casting the matrices and calculations of the solubility parameters of polymers and solvents used. Matrices of poly(dl-lactide-co-glycolide)
Nikolay N Brandt et al.
Journal of biomedical optics, 20(5), 051015-051015 (2014-12-06)
The analysis of the structure-function relationship is extremely important in the study of proteins. The importance of function-related motions of large parts or subglobules of protein molecules stimulates the spectroscopic study in the low-frequency (terahertz) domain. However, only tentative assignments
Christopher L Nobles et al.
Journal of microbiological methods, 118, 7-17 (2015-08-09)
Bacterial pathogens acquire host iron to power cellular processes and replication. Heme, an iron-containing cofactor bound to hemoglobin, is scavenged by bacterial proteins to attain iron. Methods to measure intracellular heme are laborious, involve complex chemistry, or require radioactivity. Such