A3983
Bovine Serum Albumin
lyophilized powder, essentially γ-globulin free, ≥98% (agarose gel electrophoresis)
Synonym(s):
Albumin bovine serum, BSA, Bovine albumin
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About This Item
biological source
bovine
Assay
≥98% (agarose gel electrophoresis)
form
lyophilized powder
mol wt
~66 kDa
purified by
heat shock fractionation
packaging
poly bottle of
origin
New Zealand origin
impurities
essentially globulin free
loss
≤5%
pH
7
solubility
water: soluble, clear to slightly hazy (1 g + 25 mL)
UniProt accession no.
foreign activity
Protease free
storage temp.
2-8°C
Gene Information
bovine ... ALB(280717)
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General description
Bovine Serum Albumin has three homologous domains (I, II, and III) that are connected by disulfide bonds. BSA shares structural homology with human serum albumin (HSA).
Application
Bovine Serum Albumin has been used:
- as a component of blocking solution used for fixing Drosophila embryos in immunostaining
- to block 96-deep-well plates in phage immunoprecipitation studies
- as a standard solution in fluorescence spectroscopy studies
Biochem/physiol Actions
Bovine Serum Albumin (BSA) displays intrinsic fluorescence due to the presence of two tryptophan residues. It is widely used in ligand interaction studies and in the delivery of drugs and antibodies. BSA is used as a blocking agent in enzyme-linked immunosorbent assay (ELISA).
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.
Preparation Note
Derived from New Zealand source serum
Prepared using heat shock 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
Regulatory Information
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Evaluation of biophysical interaction between newly synthesized pyrazoline pyridazine derivative and bovine serum albumin by spectroscopic and molecular docking studies
Al-Mehizia AA, et al.
Journal of Spectroscopy (New York, NY, United States), 2019 (2019)
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Current biology : CB, 29(22), 3851-3862 (2019-11-02)
In healthy individuals, injured tissues rapidly repair themselves following damage. Within a healing skin wound, recruited inflammatory cells release a multitude of bacteriocidal factors, including reactive oxygen species (ROS), to eliminate invading pathogens. Paradoxically, while these highly reactive ROS confer
Ceri-Anne E Suurmond et al.
Advanced healthcare materials, 8(24), e1901379-e1901379 (2019-11-21)
The liver has a complex and unique microenvironment with multiple cell-cell interactions and internal vascular networks. Although nonalcoholic fatty liver disease (NAFLD) is the most common chronic liver disease with multiple phases, no proper model could fully recapitulate the in
Yuhong Xiao et al.
Journal of immunological methods, 384(1-2), 148-151 (2012-06-27)
The enzyme-linked immunosorbent assay (ELISA) is an extremely common and powerful laboratory technique for detecting proteins by antibodies. Researchers frequently use bovine serum albumin (BSA) as a blocking agent to prevent non-specific binding of antigens and antibodies to the microtiter
Marcos V A S Navarro et al.
PLoS biology, 9(2), e1000588-e1000588 (2011-02-10)
The bacterial second messenger bis-(3'-5') cyclic dimeric guanosine monophosphate (c-di-GMP) has emerged as a central regulator for biofilm formation. Increased cellular c-di-GMP levels lead to stable cell attachment, which in Pseudomonas fluorescens requires the transmembrane receptor LapD. LapD exhibits a
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