| Rp. 2,991,000 |
|mol wt||~66 kDa|
|purified by||heat shock fractionation|
|loss||?5% loss on drying|
|pH||5.0-6.0 (10 mg/mL in H2O)|
|solubility||H2O: 40 mg/mL, clear to faintly turbid, faintly yellow to greenish-yellow|
|H2O: slightly soluble|
Albumin from bovine serum has been used as a test compound for detecting the weaker, distal chromatin co-associations by using enhanced 4C (e4C, enhanced chromosome conformation capture on chip) technique.
Bovine serum albumin also referred to as BSA or Fraction V is a protein isolated from cows. BSA can block vacant binding sites in enzyme-linked immunosorbent assay (ELISA) in both poly-l-lysine (PLL)-treated as well as non-treated microwells. It can also trigger insulin dependent diabetes mellitus in humans.
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.
By a modified Cohn procedure, using cold ethanol, pH and low temperature precipitation.
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.
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