Monoclonal Anti-Glycophorin A (α) antibody produced in mouse

human thymus

Monoclonal Anti-Glycophorin A (α) antibody produced in mouse is suitable for:

• agglutination assay at a working dilution of 1:800 using human erythrocytes
• flow cytometry using bone marrow nucleated cells
• indirect immunofluorescence using bone marrow nucleated cells
• western blot using extracts of human red blood cell ghosts

By immunoblotting, the antibody localizes specifically the α, αδ, α₂ bands in extracts of human red blood cell ghosts. The antibody (also cited as clone no. 15D4) binds to 8% of bone marrow nucleated cells in smears and tissue preparations using immunofluorescent microscopy or flow cytometry.

Glycophorins (GP) are sialic acid-rich polypeptides (sialoglycoproteins) that are part of the erythrocyte membrane. They are denoted α, β, γ, δ based on the decreasing molar mass. GPA and GPB are the major constituents of the red cells. They may be present as single polypeptides (α and δ), as stable homodimers (α2 and δ2) and heterodimers (αδ). Depending upon the amino acid residues at positions 1 and 5, GPA carries blood group M or N. GPA is associated exclusively with erythroid cells. It is expressed in pronormoblasts and later erythroid cells. GPA has a cytoplasmic domain that interacts with cytoskeletal structure upon induction by binding to ligand. This interaction improves RBC membrane rigidity and reduces deformability.

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