Bovine Serum Albumin

lyophilized powder, essentially IgG free, ≥96% (agarose gel electrophoresis)

Albumin bovine serum, Bovine albumin, BSA
CAS Number:
EC Number:
MDL number:

Quality Level

biological source



≥96% (agarose gel electrophoresis)


lyophilized powder

mol wt

~66 kDa

purified by

heat shock fractionation


poly bottle of


USA origin


flow cytometry: suitable
immunofluorescence: suitable


IgG free
≤25 ng/mg protein IgG




water: soluble (40 mg/ml)

storage temp.


Gene Information

bovine ... ALB(280717)

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General description

Bovine serum albumin (BSA) is a 66 kDa protein consisting of three domains with two subdomains under each. It is a α-helical, globular and non-glycosylated protein. BSA belongs to the serum albumins family. It has 17-disulfide bonds.


Bovine Serum Albumin has been used in:
  • the washing of the rabbit tissue sections in immunofluorescence microscopy
  • incubation of red blood cells (RBC) for flow cytometry analysis
  • as a component of Hanks′ balanced salt solution with Ca2+ and Mg2+ (HBSS++) for eosin-5-maleimide staining and RBC washing in magnetic circular dichroism measurements


5, 25 g in poly bottle

Biochem/physiol Actions

Bovine Serum Albumin (BSA) is a transporter for drugs, hormones and fatty acids. It is used as a blocking agent in enzyme linked immunosorbent assay (ELISA) for preventing non-specific binding of antigens and antibodies to the microtiter plates. It is a crucial component of the cell culture media and favors embryonic stem cells (hESC) differentiation. BSA shares structural features with human serum albumin. Its high solubility, low cost and purity and interaction with surfactant is exploited in cosmetic and pharmaceutical industry.
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.

Features and Benefits

  • Essentially IgG free (immunoglobulin-free)
  • Heat shock fractionated

Preparation Note

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.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Prenatal Exposure to Vinclozolin Disrupts Selective Aspects of the Gonadotrophin-Releasing Hormone Neuronal System of the Rabbit
Wadas BC, et al.
Journal of Neuroendocrinology, 22(6), 518-526 (2010)
C4d Deposits on the Surface of Red Blood Cells in Trauma Patients and Interferes with their Function
Muroya T, et al.
Critical Care Medicine, 42(5), e364-e364 (2014)
Binding of fatty acid amide amphiphiles to bovine serum albumin: role of amide hydrogen bonding
Ghosh S and Dey J
The Journal of Physical Chemistry B, 119(25), 7804-7815 (2015)
Edoardo Longo et al.
International journal of pharmaceutics, 480(1-2), 84-91 (2015-01-18)
Synchrotron radiation circular dichroism (SRCD) is a powerful tool for photo-stability assessment of proteins. Recently our research has been interested in applying SRCD to develop screening methodologies for accelerated photo-stability assessment of monoclonal antibody formulations. Despite it was proven to...
Enzyme-linked immunosorbent assay (ELISA) and blocking with bovine serum albumin (BSA)?not all BSAs are alike
Xiao Y and Isaacs SN
Journal of Immunological Methods, 384(1-2), 148-151 (2012)

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