G7900
Monoclonal Anti-Glycophorin A (α) antibody produced in mouse
ascites fluid, clone E4
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About This Item
Produtos recomendados
fonte biológica
mouse
conjugado
unconjugated
forma do anticorpo
ascites fluid
tipo de produto de anticorpo
primary antibodies
clone
E4, monoclonal
contém
15 mM sodium azide
reatividade de espécies
human
técnica(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
Isotipo
IgM
nº de adesão UniProt
Condições de expedição
dry ice
temperatura de armazenamento
−20°C
modificação pós-traducional do alvo
unmodified
Informações sobre genes
human ... GYPA(2993)
Especificidade
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.
Imunogênio
human thymus
Aplicação
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
Ações bioquímicas/fisiológicas
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.
Exoneração de responsabilidade
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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Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
nwg
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
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L L Jennings et al.
Neuropharmacology, 40(5), 722-731 (2001-04-20)
Nucleoside transport processes play an important role in human cells in salvage of nucleosides used in the biosynthesis of nucleic acids and in regulating endogenous adenosine concentrations in the human central nervous system (CNS). By altering the levels of adenosine
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
Monoclonal antibodies against glycophorins and other glycoproteins.
D J Anstee et al.
Journal of immunogenetics, 17(4-5), 301-308 (1990-08-01)
M J Telen et al.
Vox sanguinis, 52(3), 236-243 (1987-01-01)
Human erythrocyte membrane proteins express antigens which serve as markers for erythroid differentiation as well as targets for human blood group alloantibodies. We have produced and characterized a new panel of five monoclonal antibodies to erythrocyte membrane proteins. Three monoclonal
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