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Sigma-Aldrich

Albumin, Bovine Serum, Fraction V, Fatty Acid-Free

Synonym(s):

Albumin, Bovine Serum, Fraction V, Fatty Acid-Free

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About This Item

CAS Number:
9048-46-8
UNSPSC Code:
12352202
NACRES:
NA.25

Assay

≥95% (cellulose acetate electrophoresis)

form

powder

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze

impurities

≤0.02% fatty acids
≤3% ash
≤5% moisture

color

white to light yellow
light yellow to light brown

shipped in

ambient

storage temp.

2-8°C

General description

Albumin, Bovine Serum, (BSA) Fraction V, Fatty Acid-Free is useful for immunodiagnostic assays. It is designed for use in serological testing, radioimmunoassay, and hormone response studies. It is also applicable in binding and transport studies. BSA is prepared by cold ethanol extraction (Cohn method) with a pH: 6.8-7.4.
Bovine serum albumin (BSA) is a non-glycosylated globular, α-helical protein belonging to the serum albumin family. It consists of three domains with two sub-domains each and has 17-disulfide bonds.

Application

Albumin, Bovine Serum, Fraction V, Fatty Acid-Free has been used:
  • as a component of: blocking buffer immunoelectron microscopy (IEM) for various cells
  • mitochondrial isolation buffer (MIB) and mitochondria assay solution (MAS) to trap free fatty acids released during adipose tissue homogenization
  • blocking buffer for wholemount staining of the esophageal epithelium (EE) in immunofluorescence

Biochem/physiol Actions

Bovine Serum Albumin (BSA), the most vital component of cell culture media, aids in embryonic stem cells (hESC) differentiation. It aids the transportation of drugs, hormones, and fatty acids. BSA is also used as a blocking agent in enzyme-linked immunosorbent assay (ELISA).

Warning

Toxicity: Standard Handling (A)

Preparation Note

May take up to 24 h to fully dissolve.

Reconstitution

Following reconstitution, store in the refrigerator (4°C). 0.1% NaN₃ may be added as a preservative. Stock solutions are stable for up to 3 months at 4°C.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

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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M Prats
European journal of biochemistry, 75(2), 619-625 (1977-05-16)
The L-(+)-Lactate:cytochrome c oxidoreductase or cytochrome b2 from the yeasts Saccharomyces cerevisiae and Hansenula anomala were partially hydrolysed in various concentrations of trypsin. Conditions were found which allowed the isolation from the Hansenula enzyme of a 140 000 +/- 10
Andrew W Ferree et al.
Autophagy, 9(11), 1887-1896 (2013-10-24)
To study mitochondrial protein age dynamics, we targeted a time-sensitive fluorescent protein, MitoTimer, to the mitochondrial matrix. Mitochondrial age was revealed by the integrated portions of young (green) and old (red) MitoTimer protein. Mitochondrial protein age was dependent on turnover
Mohyeddine Omrane et al.
iScience, 13, 138-153 (2019-03-05)
Septins are GTP-binding proteins involved in several membrane remodeling mechanisms. They associate with membranes, presumably using a polybasic domain (PB1) that interacts with phosphoinositides (PIs). Membrane-bound septins assemble into microscopic structures that regulate membrane shape. How septins interact with PIs
Nick Osborne et al.
Current biology : CB, 18(23), 1882-1888 (2008-12-09)
The bioactive lipid sphingosine 1-phosphate (S1P) and its G protein-coupled receptors play critical roles in cardiovascular, immunological, and neural development and function. Despite its importance, many questions remain about S1P signaling, including how S1P, which is synthesized intracellularly, is released
Soyeon Park et al.
Experimental & molecular medicine, 50(8), 1-14 (2018-08-05)
Increased fatty acid (FA) is often observed in highly proliferative tumors. FAs have been shown to modulate the secretion of proteins from tumor cells, contributing to tumor survival. However, the secreted factors affected by FA have not been systematically explored.
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