Recombinant Human Glycophorin A protein (GST tag N-Terminus)
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Recombinant Human Glycophorin A protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 150 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
대체 명칭 보기
CD235a, GPA, MNS, GYPA, Glycophorin-A, MN sialoglycoprotein, PAS-2, Sialoglycoprotein alpha
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Glycophorin A protein (GST tag N-Terminus) (AB114330)
ab114330 analysed on a 12.5% SDS-PAGE gel stained with Coomassie Blue.
Reactivity 정보
서열 정보
특성 및 보관 정보
제형
Purification 테크닉
배송 시 보관 조건
적절한 단기 보관 조건
적절한 장기 보관 조건
분주 정보
보관 정보
추가 정보
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Glycophorin A interacts with other membrane proteins to form part of the membrane's skeletal protein network. This network stabilizes the erythrocyte structure and contributes to its flexibility essential for passing through narrow capillaries. Glycophorin A does not form part of any large multiprotein complex but does interact with other glycophorins such as Glycophorin B. These interactions help to form the MN and Ss blood group antigens.
Pathways
Glycophorin A is involved in several pathways including the erythrocyte development and lipid raft pathways. These pathways are important for cell signaling and membrane transport processes. Glycophorin A's role in erythrocyte development is connected to protein 4.1R which links the membrane to the underlying cytoskeleton influencing red blood cell shape and stability. Additionally its role in lipid raft-mediated signaling intersects with proteins involved in immune response regulation.
일반 정보
기능
Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane (PubMed : 35835865). Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane.. (Microbial infection) Appears to be a receptor for Hepatitis A virus (HAV).. (Microbial infection) Receptor for P.falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans.
서열 유사성
Belongs to the glycophorin A family.
Post-translational modifications
The major O-linked glycan are NeuAc-alpha-(2-3)-Gal-beta-(1-3)-[NeuAc-alpha-(2-6)]-GalNAcOH (about 78 %) and NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH (17 %). Minor O-glycans (5 %) include NeuAc-alpha-(2-3)-Gal-beta-(1-3)-[NeuAc-alpha-(2-6)]-GalNAcOH NeuAc-alpha-(2-8)-NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH. About 1% of all O-linked glycans carry blood group A, B and H determinants. They derive from a type-2 precursor core structure, Gal-beta-(1,3)-GlcNAc-beta-1-R, and the antigens are synthesized by addition of fucose (H antigen-specific) and then N-acetylgalactosamine (A antigen-specific) or galactose (B antigen-specific). Specifically O-linked-glycans are NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH-(6-1)-GlcNAc-beta-(4-1)-[Fuc-alpha-(1-2)]-Gal-beta-(3-1)-GalNAc-alpha (about 1%, B antigen-specific) and NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH-(6-1)-GlcNAc-beta-(4-1)-[Fuc-alpha-(1-2)]-Gal-beta (1 %, O antigen-, A antigen- and B antigen-specific).
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