Recombinant Human Glycophorin A protein (GST tag N-Terminus)
Be the first to review this product! Submit a review
|
(0 Publication)
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.
View Alternative Names
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 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
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.
Specifications
Form
Liquid
General info
Function
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.
Sequence similarities
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).
Target data
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com