catalog number :
MBS439060
products full name :
Glycophorin A /CD235a (Erythrocyte Marker) Mouse Monoclonal Antibody
products short name :
[Glycophorin A /CD235a]
products name syn :
[Blood group--MN locus; GPA; GPErik; GpMiIII; GPSAT; GYPA; MN sialoglycoprotein; MNS; PAS2; Sialoglycoprotein alpha]
other names :
[glycophorin-A isoform 3; Glycophorin-A; glycophorin-A; glycophorin A (MNS blood group); MN sialoglycoprotein; PAS-2; Sialoglycoprotein alpha; CD_antigen: CD235a]
products gene name :
[GYPA]
other gene names :
[GYPA; GYPA; MN; GPA; MNS; GPSAT; PAS-2; CD235a; GPErik; HGpMiV; HGpMiXI; HGpSta(C); GPA]
uniprot entry name :
GLPA_HUMAN
specificity :
Recognizes a sialoglycoprotein of 39kDa, identified as glycophorin A (GPA). It is present on red blood cells (RBC) and erythroid precursor cells. It has been shown that glycophorin acts as the receptor for Sandei virus and parvovirus. Glycophorins A (GPA) and B (GPB), which are single, trans-membrane sialoglycoproteins. GPA is the carrier of blood group M and N specificities, while GPB accounts for S and U specificities. GPA and GPB provide the cells with a large mucin like surface and it has been suggested this provides a barrier to cell fusion, so minimizing aggregation between red blood cells in the circulation.
form :
200ug/ml of Ab purified from Bioreactor Concentrate. Prepared in 10mM PBS with 0.05% BSA & 0.05% azide. Also available WITHOUT BSA & azide at 1.0mg/ml.
storage stability :
Antibody with azide - store at 2 to 8 degree C. Antibody without azide - store at -20 to -80 degree C. Antibody is stable for 24 months. Non-hazardous. No MSDS required.
tested application :
Erythrocyte Agglutination, Flow Cytometry (FC/FACS), Immunofluorescence (IF)
app notes :
Erythrocyte Agglutination. Flow Cytometry (0.5-1ug/million cells). Immunofluorescence (0.5-1ug/ml). Optimal dilution for a specific application should be determined.
other info1 :
Cellular Localization: Cell Surface. Immunogen: Human erythrocytes treated with neuraminidase
other info2 :
Hu-Chromosome Location: 4q31.22. Positive Control: Erythrocytes
products references :
Cartron JP and Rahuel C. Human erythrocyte glycophorins: protein and gene structure analyses. Transfus Med Rev 1992,6(2):63-92 Gahmberg CG et al. Biosynthesis of the major human red cell sialoglycoprotein, glycophorin A. A review. Rev Fr Transfus Immunohematol 1981,24(1):53-73 Wybenga LE et al. Glycophorin as a receptor for Sendai virus. Biochemistry 1996,35(29):9513-8 Rahuel C et al. Post-transcriptional regulation of the cell surface expression of glycophorins A, B, and E. J Biol Chem 1994, 269(52):32752-8 Thacker TC and Johnson FB. Binding of bovine parvovirus to erythrocyte membrane sialylglycoproteins. J Gen Virol 1998, 79:2163-
ncbi acc num :
NP_001295119.1
ncbi gb acc num :
NM_001308190.1
ncbi pathways :
Hematopoietic Cell Lineage Pathway (83078); Hematopoietic Cell Lineage Pathway (489); Malaria Pathway (152665); Malaria Pathway (152657)
ncbi summary :
Glycophorins A (GYPA) and B (GYPB) are major sialoglycoproteins of the human erythrocyte membrane which bear the antigenic determinants for the MN and Ss blood groups. In addition to the M or N and S or s antigens that commonly occur in all populations, about 40 related variant phenotypes have been identified. These variants include all the variants of the Miltenberger complex and several isoforms of Sta, as well as Dantu, Sat, He, Mg, and deletion variants Ena, S-s-U- and Mk. Most of the variants are the result of gene recombinations between GYPA and GYPB. [provided by RefSeq, Jul 2008]
uniprot summary :
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. 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).