Recombinant Human IgA2 protein (GST tag N-Terminus)
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Recombinant Human IgA2 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 477 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
Immunoglobulin heavy constant alpha 2, Ig alpha-2 chain C region, Ig alpha-2 chain C region BUT, Ig alpha-2 chain C region LAN, IGHA2
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human IgA2 protein (GST tag N-Terminus) (AB158743)
ab158743 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
IgA2 serves as an essential component of the mucosal immune system. It forms complexes with antigenic substances to neutralize pathogens and prevent their adherence to epithelial cells. The dimeric form of IgA2 combined with the secretory component allows it to be effectively transported across mucosal barriers into secretions where it functions without activating complement pathways therefore reducing inflammation. The secretory IgA2 forms a physical barrier on mucosal surfaces trapping microbes and toxins.
Pathways
IgA2 functions within the mucosal immune response pathways and plays an important interaction role with components of the adaptive immune response. It associates with the polymeric immunoglobulin receptor (pIgR) facilitating its transcytosis across epithelial cells into secretions. IgA2 also operates within the immunological network alongside J chain proteins instrumental in forming its dimeric structure important for appropriate secretion and function in mucosal immunity.
Specifications
Form
Liquid
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). Ig alpha is the major immunoglobulin class in body secretions (PubMed : 2241915).
Target data
Product promise
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