Recombinant Human IgG1 Fc Protein, His Tag (Active) is a Human Fragment protein, in the 99 to 330 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes The reducing (R) protein migrates as 30-33 kDa in SDS-PAGE due to glycosylation. |
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.
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
Recombinant Human IgG1 Fc Protein, His Tag (Active) is a Human Fragment protein, in the 99 to 330 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
pH: 7.4
Constituents: Glycine, L-Arginine, Sodium chloride, 5% Trehalose, 0.61% Tris
Purified by Immobilized metal affinity chromatography.
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.
Glycosylation on Asn-180 is required for interaction with Fc receptors and ability to activate the complement pathway.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
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SDS-PAGE of reduced ab219660 stained overnight with Coomassie Blue. The protein migrates at 30-33 kDa due to glycosylation.
Loaded Biotinylated Human CD64, His,Avitag on SA Biosensor, can bind ab219660 with an affinity constant of 1.60 nM as determined in BLI assay.
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