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  • G7900 - Monoclonal Anti-Glycophorin A (α) antibody produced in mouse

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G7900 Sigma

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

ascites fluid, clone E4

Properties

Related Categories Alphabetical Index, Antibodies, Antibodies to Human Plasma Proteins, GD-GL, Primary Antibodies,
species reactivity   human
application(s)   agglutination assay: 1:800 using human erythrocytes
  flow cytometry: suitable using bone marrow nucleated cells
  indirect immunofluorescence: suitable using bone marrow nucleated cells
  western blot: suitable using extracts of human red blood cell ghosts
clone   E4, monoclonal
antibody form   ascites fluid
isotype   IgM
contains   15 mM sodium azide
shipped in   dry ice
storage temp.   −20°C
Gene Information   human ... GYPA(2993)
biological source   mouse
conjugate   unconjugated

Description

Immunogen

human thymus

Specificity

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.

Application

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

Biochem/physiol Actions

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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