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CD235a/Glycophorin A [GYPA/280]

Product information References Bioinformatics Documents
Product group: Primary
Monoclonal/ Polyclonal: Monoclonal
Clone: GYPA/280
Host: Mouse
Isotype: IgG1
Application: Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC)
Application notes: Prediluted
Conjugation Type: Unconjugated
Lightchain type: Kappa
Reactivity: Human
General notes: Localization: membrane.
Buffer: citrate pH6.0
UNSPSC code: 12352203

CD235a or Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). Strongly labels normal erythroid cells at all stages of differentiation from the erythroblast to the mature red cell and does not react with glycophorin B. (Shipping Cost: €200.00)

CD235a/Glycophorin A [GYPA/280]

CD235a or Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). Strongly labels normal erythroid cells at all stages of differentiation from the erythroblast to the mature red cell and does not react with glycophorin B.