Skip to Content
MilliporeSigma
All Photos(1)

Documents

SAB3700018

Sigma-Aldrich

Anti-Bovine IgG (Fc specific) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sign Into View Organizational & Contract Pricing


About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

bovine

concentration

1.8 mg/mL

technique(s)

immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

Related Categories

General description

Immunoglobulin G (IgG), a member of the immunoglobulin family, is a widely expressed serum antibody. It consists of a γ heavy chain in the constant (C) region. The monomeric 150kDa structure of IgG constitutes two identical heavy chains and two identical light chains. The primary structure of IgG also contains disulfide bonds involved in linking the two heavy chains, linking the heavy and light chains and resides inside the chains. IgG is further subdivided into four classes namely, IgG1, IgG2, IgG3, and IgG4 with different heavy chains, named γ1, γ2, γ3, and γ4, respectively. Limited digestion using papain cleaves the antibody into three fragments, two of which are identical and contain the antigen-binding activity. The third fragment does not possess antigen-binding activity and is known as fragment crystallizable (Fc). It interacts with cells and effector molecules. The Fc fragment contains the CH2 and CH3 domains of the antibody molecule. Maternal IgG is the only antibody transported across the placenta to the fetus. It passively immunizes the infants.

Specificity

This product was prepared from monospecific antiserum by immunoaffinity chromatography using Bovine IgG coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Rabbit Serum, Bovine IgG, Bovine IgG F(c) and Bovine Serum. No reaction was observed against Bovine IgG F(ab′)2.

Immunogen

Bovine IgG F(c) fragment

Application

Anti-Bovine IgG (Fc specific) antibody produced in rabbit has been used in Western Blotting.

Physical properties

Antibody format: IgG

Physical form

Supplied in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2

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.

Not finding the right product?  

Try our Product Selector Tool.

Storage Class

10 - Combustible liquids

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Two novel cross?protective antigens for bovine Pasteurella multocida
Huihui DU
Molecular Medicine Reports, 16(4), 4627-4633 (2017)
Huihui Du et al.
Molecular medicine reports, 16(4), 4627-4633 (2017-08-10)
Pasteurella multocida is an important pathogen that leads to a range of diseases that have severe economic consequences on cattle production. In order to develop an effective cross‑protective component vaccine, an immunoproteomics approach was used to analyze outer membrane proteins
Human placental Fc receptors and the transmission of antibodies from mother to fetus.
Simister NE and Story CM
Journal of Reproductive Immunology, 37(1), 1-23 (1997)
Antibody structure, instability, and formulation.
Wang W
Journal of Pharmaceutical Sciences, 96(1), 1-26 (2007)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service