| 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. |
| 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. 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. Mediates IgG effector functions on monocytes triggering ADCC of virus-infected cells. |
| Protein Name | Immunoglobulin Heavy Constant Gamma 1Ig Gamma-1 Chain C RegionIg Gamma-1 Chain C Region EuIg Gamma-1 Chain C Region KolIg Gamma-1 Chain C Region Nie |
| Cellular Localisation | Isoform 1: SecretedIsoform 2: Cell MembraneSingle-Pass Membrane Protein |
| Alternative Antibody Names | Anti-Immunoglobulin Heavy Constant Gamma 1 antibodyAnti-Ig Gamma-1 Chain C Region antibodyAnti-Ig Gamma-1 Chain C Region Eu antibodyAnti-Ig Gamma-1 Chain C Region Kol antibodyAnti-Ig Gamma-1 Chain C Region Nie antibodyAnti-IGHG1 antibody |
Information sourced from Uniprot.org
