Key features and details
- Mouse monoclonal [HI264] to Glycophorin A (APC)
- Suitable for: Flow Cyt
- Reacts with: Human
- Conjugation: APC. Ex: 645nm, Em: 660nm
- Isotype: IgG2a
Product nameAnti-Glycophorin A antibody [HI264] (APC)
See all Glycophorin A primary antibodies
DescriptionMouse monoclonal [HI264] to Glycophorin A (APC)
ConjugationAPC. Ex: 645nm, Em: 660nm
SpecificityIn indirect agglutination tests ab91163 reacts with normoblasts and erythrocytes. No reaction occurs with En(a-) erythrocytes and other normal peripheral blood cells.
Tested applicationsSuitable for: Flow Cytmore details
Species reactivityReacts with: Human
Synthetic peptide (N terminal) from Human Glycophorin A.
- Cells from normal Human bone marrow.
Storage instructionsShipped at 4°C. Store at +4°C.
Storage bufferpH: 7.20
Preservative: 0.09% Sodium azide
Constituent: 1% BSA
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab91163 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|Flow Cyt||Use 20µl for 106 cells.
ab91364 - Mouse monoclonal IgG2a, is suitable for use as an isotype control with this antibody.
FunctionGlycophorin 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. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV).
Sequence similaritiesBelongs to the glycophorin A family.
modificationsThe 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).
Cellular localizationCell membrane. Appears to be colocalized with SLC4A1.
- Information by UniProt
- AI853584 antibody
- Blood group--MN locus antibody
- CD_antigen=CD235a antibody
ab91163 has been referenced in 1 publication.
- Awojoodu AO et al. Acid sphingomyelinase is activated in sickle cell erythrocytes and contributes to inflammatory microparticle generation in SCD. Blood 124:1941-50 (2014). PubMed: 25075126