G7900
Monoclonal Anti-Glycophorin A (α) antibody produced in mouse
ascites fluid, clone E4
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About This Item
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biological source
mouse
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
E4, monoclonal
contains
15 mM sodium azide
species reactivity
human
technique(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
isotype
IgM
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... GYPA(2993)
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.
Immunogen
human thymus
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.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class
10 - Combustible liquids
wgk_germany
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
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J A Chasis et al.
The Journal of clinical investigation, 75(6), 1919-1926 (1985-06-01)
Erythrocyte skeletal proteins are known to play an important role in determining membrane deformability. In order to see whether transmembrane proteins also influence deformability and, if so, whether this influence is mediated by an interaction with the membrane skeleton, we
D J Anstee
Vox sanguinis, 58(1), 1-20 (1990-01-01)
The surface of the human red blood cell is dominated by a small number of abundant blood group active proteins. The major proteins are the anion transport protein (band 3) which has AB(H) activity, and Glycophorin A which has MN
Structure and function of the red cell membrane sialoglycoproteins.
D J Anstee et al.
British journal of haematology, 64(2), 211-215 (1986-10-01)
Bishwanath Kumar Chourasia et al.
Infection and immunity, 88(2) (2019-11-13)
Cytoadherence-linked asexual gene 9 (Clag9), a conserved Plasmodium protein expressed during the asexual blood stages, is involved in the cytoadherence of infected red blood cells (RBCs) to the endothelial lining of blood vessels. Here, we show that Plasmodium falciparum Clag9
M J Telen et al.
Transfusion, 27(4), 309-314 (1987-07-01)
The minor red cell sialoglycoproteins--beta and gamma (also known as glycophorin C)--are believed to be important to the structural integrity of red cells. The absence of sialoglycoproteins alpha and delta, as seen in En(a-) and S-s-U- cells, respectively, results in
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