CD235a (Glycophorin A) (Cytoplasmic domain) (clone BRIC 163) PE, anti-human

Decription:
Mouse monoclonal antibody to human Glycophorin A (Cytoplasmic Domain) PE conjugate. Glycophorin A (GPA) (Mr 43kDa as a monomer and 86kDa as a dimer) is the major sialoglycoprotein of human erythrocytes and is the most abundant, together with band 3 (anion transporter protein), with which it appears to be associated. The complete amino acid sequence and sites of glycosylation are known. GPA consists of 131 amino acids, which constitute three domains: (i) a heavily glycosylated N-terminal extracellular domain of 72 amino acids, (ii) a hydrophobic intramembranous domain of 23 amino acids, and (iii) a C-terminal cytoplasmic domain of 36 amino acids1,. GPA is generally present in the membrane in dimeric form, with the polypeptides associated at the hydrophobic intramembranous domain. It probably complexes with other membrane glycoproteins. GPA is a marker for erythroid cells. There are about 3-12 x 105 GPA molecules per erythrocyte. Rare individuals lacking GPA are known.

Synonyms: GPA, Glycophorin A, CD235a, 1F5, HRF20, MN sialoglycoprotein, GYPA, HGpMiV, HGpMiXI, MNS, GPSAT

Clone: BRIC 163

Isotype: Mouse IgG2a kappa light chain

Immunogen: BRIC 163 was made in response to Triton X-100 soluble fraction of erythrocyte membranes. Marker for erythroid cells. There are about 2-10x105 GPA molecules per erythrocyte.

Reactivity: human

Form: PE-conjugate, in PBS buffer, pH 7.2 containing 0.1% sodium azide, 1% BSA

Applications: Flow Cytometry

Working Dilution: ul per test

Storage: 2-8C, do not freeze

References:
Anstee, D.J. (1990) Vox Sang. 58: 1-20 (review)
Daniels, G. (1995) Human Blood groups, Blackwell Science, Oxford
Okubo Y., et al. (1988) Vox Sang. 54: 107-111