G7900
Monoclonal Anti-Glycophorin A (α) antibody produced in mouse
ascites fluid, clone E4
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About This Item
Prodotti consigliati
Origine biologica
mouse
Coniugato
unconjugated
Forma dell’anticorpo
ascites fluid
Tipo di anticorpo
primary antibodies
Clone
E4, monoclonal
contiene
15 mM sodium azide
Reattività contro le specie
human
tecniche
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
N° accesso UniProt
Condizioni di spedizione
dry ice
Temperatura di conservazione
−20°C
modifica post-traduzionali bersaglio
unmodified
Informazioni sul gene
human ... GYPA(2993)
Specificità
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.
Immunogeno
human thymus
Applicazioni
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
Azioni biochim/fisiol
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.
Esclusione di responsabilità
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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Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
nwg
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°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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