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G7650

Sigma-Aldrich

Anti-Glycophorin A,B (α,δ) antibody, Mouse monoclonal

clone E3, purified from hybridoma cell culture

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

E3, monoclonal

species reactivity

human

technique(s)

agglutination assay: 1:400
flow cytometry: suitable using bone marrow nucleated cells
indirect immunofluorescence: suitable using bone marrow nucleated cells
western blot: 0.5-1 μg/mL using extracts of red blood cell ghosts2

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

Specificity

By immunoblotting, the antibody localizes specifically the α, δ, αδ, α2, δ2, α2δ and α3 bands in extracts of human red blood cell ghosts. The antibody (also cited as clone no. 6H5) binds to 12% of bone marrow nucleated cells in smears and tissue preparations using immunofluorescent microscopy or flow cytometry.

Immunogen

human thymus

Application

Monoclonal Anti-Glycophorin A,B (α, δ) antibody produced in mouse is suitable for:
  • immunoblot analysis to monitor the shaving completion of human RBC membrane protein components on the cytoplasmic surface, the extracellular surface, and the erythrocyte cytoskeleton.
  • immunoprecipitation of glycophorin A/B from erythrocyte membrane lysate.
The antibody is suitable for localization of glycophorins A and B using:
  • immunoblot analysis at a working concentration of 0.5-1μg/mL with extracts of red blood cell ghosts
  • indirect immunofluorescence and flow cytometry with bone marrow nucleated cells.
It is also suitable for use in agglutination assay at a working dilution of 1:400.

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. Based on the aminoacid substitution at residue 29, GPB carries blood group N and S activity. GPA is associated exclusively with erythroid cells. It is expressed in pronormoblasts and later erythroid cells.

Physical form

Solution in 0.1 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

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 Code

12 - Non Combustible Liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

含少量动物源组分生物产品
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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)
Laty G Thiam et al.
Scientific reports, 11(1), 7129-7129 (2021-03-31)
Human erythrocytes are indispensable for Plasmodium falciparum development. Unlike other eukaryotic cells, there is no existing erythroid cell line capable of supporting long-term P. falciparum in vitro experiments. Consequently, invasion phenotyping experiments rely on erythrocytes of different individuals. However, the
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
Henrietta E Mensah-Brown et al.
The Journal of infectious diseases, 212(8), 1288-1297 (2015-04-04)
Plasmodium falciparum invades human erythrocytes by using an array of ligands that interact with several receptors, including sialic acid (SA), complement receptor 1 (CR1), and basigin. We hypothesized that in malaria-endemic areas, parasites vary invasion pathways under immune pressure. Therefore
Rouger, P., and Anstee, D.
Vox Sanguinis, 55, 57-57 (1988)

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