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I2136

Sigma-Aldrich

Anti-Human IgG (Fc specific) antibody produced in goat

affinity isolated antibody, buffered aqueous solution

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Synonym(s):
Anti Human IgG Fc - Anti-Human IgG (Fc specific) antibody produced in goat, Anti Human Igg, Anti Human Igg Antibody, Anti-Human Igg, Anti-Human Igg Fc, Goat Anti Human Igg
MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

goat

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

technique(s)

indirect ELISA: 1:10,000

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

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General description

The product binds human IgG and does not bind other human Igs.
Immunoglobulins comprise of two fragment antigen binding (Fab) and one fragment crystallizable (Fc) domains. The gene encoding IgG gene cluster is located on human chromosome 14.
Anti-Human IgG (Fc specific) antiserum is produced in goat using purified human IgG, Fc fragment, as the immunogen. Affinity isolated antibody is obtained from goat anti-human IgG antiserum by immunospecific purification which removes essentially all goat serum proteins, including immunoglobulins, which do not specifically bind to the Fc fragment of human IgG.

Specificity

Specificity for the Fc fragment of human IgG is determined by ELISA and immunoelectrophoresis (IEP). The antibody preparation is specific for human IgG, Fc fragment when tested against purified human IgA, IgG (Fc and Fab fragments), IgM, Bence Jones kappa, and Bence Jones lambda myeloma proteins. No reactivity is observed with the Fab fragment of human IgG, light chains, IgA, or IgM. The affinity purified anti-human IgG (Fc specific) reagent offers the advantage of increased sensitivity for human IgG without cross reactivity with other substances present on membrane or cell surface. The lack of interspecies cross reactivity with mouse or rat serum proteins makes this product excellent for the screening of human monoclonal antibodies produced by hybridoma cells grown in vivo in mouse or rat ascites fluids. This product has the ability to detect all human IgG subclasses in human biological fluids or tissues of normal or pathological situations such as cancer or autoimmune diseases. It is effective as a second antibody reagent in immunoassay procedures and can be used as starting material for conjugates using enzymes or fluorescent dyes.

Immunogen

Anti-Human IgG (Fc specific) antiserum is produced in goat using purified human IgG, Fc fragment, as the immunogen

Application

Anti-Human IgG (Fc specific) antibody produced in goat has been used:
  • in double-capture ELISA to measure antiglobulin responses in serum of transplant patients treated with CD52 monoclonal antibodies (CAMPATH-1G)
  • in detection of IgG levels rheumatoid arthritis patients
  • in small intestine biopsies
  • in patients with acute myocardial infarction by immunoblotting
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Enzyme-linked immunosorbent assay (1 paper)

Biochem/physiol Actions

IgG antibody subtype is the most abundant of serum immunoglobulins of the immune system. It is secreted by B cells and is found in blood and extracellular fluids and provides protection from infections caused by bacteria, fungi and viruses. Maternal IgG is transferred to fetus through the placenta that is vital for immune defense of the neonate against infections. Mutations in the Fc region of IgG is implicated in autoimmune diseases like Rheumatoid arthritis. Engineered Fc proteins have therapeutic significance for the treatment of autoimmune diseases.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide

Storage and Stability

For continuous use, store at 2-8 °C for up to one month. For extended storage, the solution may be frozen in working aliquots. Repeated freezing and thawing, or storage in "frost-free" freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use.

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.

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificates of Analysis (COA)

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Engineering the fragment crystallizable (Fc) region of human IgG1 multimers and monomers to fine-tune interactions with sialic acid-dependent receptors.
Blundell P A, et al.
The Journal of Biological Chemistry, jbc-M117 (2017)
Stanislav Melnik et al.
Plant biotechnology journal, 16(1), 27-38 (2017-04-20)
Antibody MC10E7 is one of a small number of monoclonal antibodies that bind specifically to [Arg4]-microcystins, and it can be used to survey natural water sources and food samples for algal toxin contamination. However, the development of sensitive immunoassays in
The structure of a typical antibody molecule
Travers P, et al.
Immunobiology: The Immune System in Health and Disease (2001)
Peter Brünker et al.
Molecular cancer therapeutics, 15(5), 946-957 (2016-04-03)
Dysregulated cellular apoptosis and resistance to cell death are hallmarks of neoplastic initiation and disease progression. Therefore, the development of agents that overcome apoptosis dysregulation in tumor cells is an attractive therapeutic approach. Activation of the extrinsic apoptotic pathway is
Elin Lunde et al.
BMC biotechnology, 10, 61-61 (2010-08-26)
Whereas T cell receptors (TCRs) detect peptide/major histocompatibility complexes (pMHCs) with exquisite specificity, there are challenges regarding their expression and use as soluble detection molecules due to molecular instability. We have investigated strategies for the production of TCR-immunoglobulin (Ig) fusion

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