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B2901

Sigma-Aldrich

Monoclonal Anti-Bovine Serum Albumin antibody produced in mouse

clone BSA-33, ascites fluid

Synonym(s):
Anti-BSA, Anti Bsa, Anti-Albumin, bovine serum, Bsa Antibody, BSA Antibody - Monoclonal Anti-Bovine Serum Albumin antibody produced in mouse, Anti-Bsa Antibody
MDL number:
NACRES:
NA.46

Quality Level

biological source

mouse

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

BSA-33, monoclonal

contains

15 mM sodium azide

species reactivity

turkey (low), goat (high), horse (low), bovine (high), canine (low), sheep (high)

should not react with

hamster, pig, guinea pig, feline, rat, human, donkey, rabbit, mouse, chicken, pigeon

technique(s)

dot blot: suitable
indirect ELISA: 1:1,000

isotype

IgG2a

shipped in

dry ice

storage temp.

−20°C

Gene Information

bovine ... Alb(280717)
chicken ... Alb(396197)
dog ... Alb(403550)
horse ... Alb(100034206)
human ... ALB(213)
mouse ... Alb(11657)
pig ... Alb(396960)
rabbit ... Alb(100009195)
rat ... Alb(24186)
sheep ... Alb(443393)

General description

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

Specificity

Bovine serum albumin (BSA) is the main protein synthesized in the liver that constitutes over 50% of total serum proteins.
Monoclonal Anti-Bovine Serum Albumin antibody is specific for SDS-denatured and reduced BSA. While the product is highly cross reactive with goat and sheep serum; it has a lower affinity for dog, turkey and horse serum albumins.

Immunogen

Bovine serum albumin

Application

Monoclonal Anti-Bovine Serum Albumin has been used in:
  • enzyme linked immunosorbent assays (ELISA)
  • competitive ELISA
  • immunodot blot
  • western blotting
  • immunoaffinity purification or adsorption of BSA from biological fluids.

Biochem/physiol Actions

Bovine serum albumin (BSA) is often used as a protein standard and can also be used in cell culture media, forensics, and foodstuffs preparation. It also acts as a transporter for drugs, hormones and fatty acids.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Origin

Enter Lot Number to search for Certificate of Origin (COO).

Molecular identification, immunolocalization, and functional activity of a vacuolar-type H+-ATPase in bovine rumen epithelium
Albrecht E, et al.
Journal of Comparative Physiology. B, Biochemical, Systemic, and Environmental Physiology, 178(2), 285-295 (2008)
Daniel M Houslay et al.
Science signaling, 9(441), ra82-ra82 (2016-08-18)
Class I phosphoinositide 3-kinases (PI3Ks) catalyze production of the lipid messenger phosphatidylinositol 3,4,5-trisphosphate (PIP3), which plays a central role in a complex signaling network regulating cell growth, survival, and movement. This network is overactivated in cancer and inflammation, and there
Reversibility of scrapie-associated prion protein aggregation.
Callahan, et al.
The Journal of Biological Chemistry, 276, 28022-28028 (2021)
Fatty acids of Treponema pallidum and Borrelia burgdorferi lipoproteins
Belisle JT, et al.
Journal of Bacteriology, 176(2), 2151-2157 (1994)
J T Belisle et al.
Journal of bacteriology, 176(8), 2151-2157 (1994-04-01)
A fundamental ultrastructural feature shared by the spirochetal pathogens Treponema pallidum subsp. pallidum (T. pallidum) and Borrelia burgdorferi, the etiological agents of venereal syphilis and Lyme disease, respectively, is that their most abundant membrane proteins contain covalently attached fatty acids.

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