Recombinant Human IGHG1 Protein
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Recombinant Human IGHG1 Protein is a Human Full Length protein, in the 1 to 330 aa range, expressed in HEK 293 cells, with >95%, suitable for SDS-PAGE.
View Alternative Names
Immunoglobulin heavy constant gamma 1, Ig gamma-1 chain C region, Ig gamma-1 chain C region EU, Ig gamma-1 chain C region KOL, Ig gamma-1 chain C region NIE, IGHG1
- SDS-PAGE
Lab
SDS-PAGE - Recombinant Human IGHG1 Protein (AB283421)
SDS-page analysis of ab283421
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
IgG antibodies function as an important component of the adaptive immune system. They form part of complex immune responses where they help in antigen recognition and neutralization. These antibodies can opsonize pathogens making them more recognizable to phagocytes for destruction. IgG also activates the complement system which contributes to the lysis of pathogenic cells. As a bridge between innate and adaptive immunity IgG mediates the interaction with natural killer (NK) cells enhancing the cell-mediated immune response.
Pathways
The signaling pathways involving IgG antibodies include the classical complement pathway and Fc receptor signaling. The classical complement pathway complements the antibodies in opsonizing pathogens promoting inflammation and leading to the lysis of pathogens. Fc receptors on immune cells recognize and bind to the Fc region of IgG triggering phagocytosis and the cytotoxic activity of immune effector cells. IgG is related to other proteins such as complement proteins and Fcγ receptors which are essential for its role in immune signaling.
Specifications
Form
Lyophilized
General info
Function
Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed : 20176268, PubMed : 22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed : 17576170, PubMed : 20176268). Mediates IgG effector functions on monocytes triggering ADCC of virus-infected cells.
Post-translational modifications
Glycosylation on Asn-180 is required for interaction with Fc receptors and ability to activate the complement pathway.. (Microbial infection) Deglycosylation on Asn-180 by S.pyogenes EndoS or Endos2 endoglucosidases prevents interaction between immunoglobulin-gamma (IgG) and Fc receptors, impairing ability to activate the complement pathway.
Target data
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Product promise
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