CD235a (Glycophorin A) (Extracellular domain) (clone BRIC256) PE, anti-human

Decription:
Mouse monoclonal antibody to human Glycophorin A (extracellular 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: BRIC256

Isotype: Mouse IgG1 kappa light chain

Immunogen: Glycophorin A (GPA) Mr 43kDa as a monomer and 86kDa as a dimer.

Reactivity: human

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

Applications: Flow Cytometry, Immunofluorescence

Working Dilution: 2ul per test (may change from lot to lot)

Storage: 2-8C, do not freeze

References:
1. Anstee, D.J. (1990) Vox Sang. 58: 1-20 (review)
2. Gardner, B., et al. (1989) Immunology 68: 283-289.
3. Lloyd-Evans et al (1999) Transfusion Medicine 9 155-160
4. Rouger P Muller JY (eds) (1997) Proceedings of the third International workshop and symposium on monoclonal antibodies against human red cells and related antigens, Nantes 1996 4 No. 1