Recombinant Human IGHG1 Protein is a Human Full Length protein, in the 1 to 330 aa range, expressed in HEK 293, with >=95% purity and suitable for SDS-PAGE.
>=95% SDS-PAGE
HEK 293 cells
Tag free
SDS-PAGE
No
A S T K G P S V F P L A P S S K S T S G G T A A L G C L V K D Y F P E P V T V S W N S G A L T S G V H T F P A V L Q S S G L Y S L S S V V T V P S S S L G T Q T Y I C N V N H K P S N T K V D K K V E P K S C D K T H T C P P C P A P E L L G G P S V F L F P P K P K D T L M I S R T P E V T C V V V D V S H E D P E V K F N W Y V D G V E V H N A K T K P R E E Q Y N S T Y R V V S V L T V L H Q D W L N G K E Y K C K V S N K A L P A P I E K T I S K A K G Q P R E P Q V Y T L P P S R D E L T K N Q V S L T C L V K G F Y P S D I A V E W E S N G Q P E N N Y K T T P P V L D S D G S F F L Y S K L T V D K S R W Q Q G N V F S C S V M H E A L H N H Y T Q K S L S L S P G K
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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 IGHG1 Protein is a Human Full Length protein, in the 1 to 330 aa range, expressed in HEK 293, with >=95% purity and suitable for SDS-PAGE.
>=95% SDS-PAGE
HEK 293 cells
Tag free
SDS-PAGE
No
Yes
Yes
Human
Reconstitute in PBS
pH: 7.4
Constituents: 10.26% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic
A S T K G P S V F P L A P S S K S T S G G T A A L G C L V K D Y F P E P V T V S W N S G A L T S G V H T F P A V L Q S S G L Y S L S S V V T V P S S S L G T Q T Y I C N V N H K P S N T K V D K K V E P K S C D K T H T C P P C P A P E L L G G P S V F L F P P K P K D T L M I S R T P E V T C V V V D V S H E D P E V K F N W Y V D G V E V H N A K T K P R E E Q Y N S T Y R V V S V L T V L H Q D W L N G K E Y K C K V S N K A L P A P I E K T I S K A K G Q P R E P Q V Y T L P P S R D E L T K N Q V S L T C L V K G F Y P S D I A V E W E S N G Q P E N N Y K T T P P V L D S D G S F F L Y S K L T V D K S R W Q Q G N V F S C S V M H E A L H N H Y T Q K S L S L S P G K
Full Length
36 kDa
1 to 330
Recombinant
Lyophilized
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.
Ambient - Can Ship with Ice
Ambient
Ambient
This supplementary information is collated from multiple sources and compiled automatically.
Immunoglobulin G (IgG) often referred to as IgG is the most common type of antibody found in blood circulation. It is an important element of the immune response enabling the body to identify and neutralize pathogens such as bacteria and viruses. IgG antibodies have a molecular weight of approximately 150 kDa. They are produced by B cells and are distributed predominantly in blood and extracellular fluid allowing them to play a significant role in immunity. IgG antibodies come in four subclasses: IgG1 IgG2 IgG3 and IgG4 each differing in their heavy chain structure and effector functions.
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.
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.
Elevated or diminished levels of IgG are associated with conditions like autoimmune diseases and immunodeficiencies. For example rheumatoid arthritis can involve abnormal IgG response where alterations in Fc glycosylation impact its function connecting IgG to the disorder. In immunodeficiencies such as common variable immunodeficiency (CVID) patients may have low levels of IgG leading to increased susceptibility to infections. IgG in these diseases interacts with proteins like cytokines and immune receptors influencing disease progression.
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