Mouse monoclonal antibody to human Glycophorin A (Cytoplasmic Domain) Affinity purified. 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.
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.
Isotype
Mouse IgG2a kappa light chain
Reactivity
Human
Applications
IHC, WB
Form
Affinity purified, in 0.1 M glycine buffer, 1 M Tris buffer, pH 7.4, sterile filtered
Storage
2-8C for immediate use, or at -2°C (aliquot)
References
1. Anstee, D.J. (1990) Vox Sang. 58: 1-20 (review) 2. Daniels, G. (1995) Human Blood groups, Blackwell Science, Oxford 3. Okubo Y., et al. (1988) Vox Sang. 54: 107-111
Supplier
ARP
View product citations for antibody 08-9410-2 on CiteAb
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