Native Human IgG protein is a Human Full Length protein with >95% purity and suitable for SDS-PAGE.. The predicted molecular weight of ab91102 native protein is 150 kDa
- Save time and ensure accurate results - use our IgG protein as an isotype control
- No cross-reaction from other immunoglobulin isotypes
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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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.
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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
Native Human IgG protein is a Human Full Length protein with >95% purity and suitable for SDS-PAGE.. The predicted molecular weight of ab91102 native protein is 150 kDa
- Save time and ensure accurate results - use our IgG protein as an isotype control
- No cross-reaction from other immunoglobulin isotypes
pH: 7.4
Preservative: 0.05% Sodium azide
Constituents: Phosphate Buffer, 0.87% Sodium chloride
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.
Protein Determination: Extinction Coefficient (E) 0.1% at 280nm, 1cm pathway = 1.36.
Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
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SDS-PAGE: 4-12% Bis-Tris NuPAGE gel
Lane 1. Molecular weight markers
Lane 2. 5 μg IgG (reduced/heated)
Lane 3. 10 μg IgG (reduced/heated)
Lane 4. 20 μg IgG (reduced/heated)
Lane 5. 5 μg IgG (non-reduced/no heat)
Lane 6. 10 μg IgG non-reduced/no heat)
Lane 7. 20 μg IgG non-reduced/no heat)
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