A8531
Bovine Serum Albumin
pH <5.0, powder
Synonym(s):
Albumin bovine serum, BSA, Bovine albumin
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About This Item
Recommended Products
biological source
bovine
Quality Level
form
powder
mol wt
~66 kDa
~66,000
packaging
vial of 50 mg
origin
USA origin
technique(s)
ELISA: suitable
gel permeation chromatography (GPC): suitable
immunohistochemistry: suitable
impurities
~0.3% dithiothreitol
pH
<5.0
suitability
suitable for (Suitable for use as a gel filtration marker)
UniProt accession no.
foreign activity
BT virus, none detected
VSV virus, none detected
storage temp.
−20°C
Gene Information
bovine ... ALB(280717)
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General description
Albumin is the most abundant plasma protein in humans. It has a molecular mass of 66.5 kDa.
Application
Albumin from bovine serum has been used:
- for blocking of nonspecific immunoglobulin during immunohistochemical reactions.
- to coat microplates for blocking non-specific binding during I-ELISA (Indirect Enzyme-linked Immunosorbent Assay)
- as molecular mass standard in analytical gel filtration chromatography for Superdex® 75 10/300 GL gel filtration column.
- for measuring fluorescence for PR1 (phytofluor red 1) by using Fluorescence correlation spectroscopy (FCS)
- as a reference mixture along with horse Mb in Size Exclusion Chromatography
Gel filtration molecular weight marker
Biochem/physiol Actions
Bovine serum albumin also refers 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 and non-treated microwells. It can also triggers the insulin dependent diabetes mellitus.
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.
High levels of albumin are associated with dehydration. Albumin turnover is seen in infants with iron deficiency anemia. Albumin in serum level is associated with advanced liver disease.
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.
Legal Information
Superdex is a registered trademark of Cytiva
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificates of Analysis (COA)
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UCAN US
Rev. Med. Vet. (Toulouse), 161(2), 51-56 (2010)
Abigail E Miller et al.
Proceedings of the National Academy of Sciences of the United States of America, 103(30), 11136-11141 (2006-07-18)
Fluorescence correlation spectroscopy (FCS) was used to investigate the hydrodynamic and photophysical properties of PR1 (phytofluor red 1), an intensely red fluorescent biliprotein variant of the truncated cyanobacterial phytochrome 1 (Cph1Delta, which consists of the N-terminal 514 amino acids). Single-molecule
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Caenorhabditis elegans gelsolin-like protein-1 (GSNL-1) is a new member of the gelsolin family of actin regulatory proteins [Klaavuniemi, T., Yamashiro, S., and Ono, S. (2008) J. Biol. Chem. 283, 26071-26080]. It is an unconventional gelsolin-related protein with four gelsolin-like (G)
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The expression of immune response in the form of leukocytic infiltrate by CD3+, CD4+, and CD8+ cells in the epithelium and in the intestinal lamina propria of chicks was studied in the present work by means of immunohistochemical reaction. The
Y Qiu et al.
The Journal of biological chemistry, 273(36), 23426-23432 (1998-08-29)
Myoglobin (Mb) has been believed to be absent generally from mammalian smooth muscle tissue. Examination of human rectal, uterine, bladder, colon, small intestine, arterial, and venous smooth muscle by immunohistochemical techniques shows that each of these tissues is immunopositive for
Protocols
Gel filtration chromatography is an established method for determining the size and molecular mass of proteins.
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