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GYPA / CD235a / Glycophorin A Antibody (C-Terminus)
Goat Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | P02724 |
| Reactivity | Human |
| Host | Goat |
| Clonality | Polyclonal |
| Calculated MW | 16kDa |
| Dilution | ELISA (1:4000), IHC-P (2 µg/ml), WB (1-3 µg/ml) |
| Gene ID | 2993 |
|---|---|
| Other Names | Glycophorin-A, MN sialoglycoprotein, PAS-2, Sialoglycoprotein alpha, CD235a, GYPA, GPA |
| Target/Specificity | Human GYPA / Glycophorin A. |
| Reconstitution & Storage | Store at -20°C. Minimize freezing and thawing. |
| Precautions | GYPA / CD235a / Glycophorin A Antibody (C-Terminus) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | GYPA (HGNC:4702) |
|---|---|
| Synonyms | GPA |
| Function | Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane (PubMed:35835865). 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. |
| Cellular Location | Cell membrane; Single-pass type I membrane protein Note=Appears to be colocalized with SLC4A1 |
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Provided below are standard protocols that you may find useful for product applications.
Background
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).
References
Siebert P.D.,et al.Proc. Natl. Acad. Sci. U.S.A. 83:1665-1669(1986).
Tate C.G.,et al.Biochem. J. 254:743-750(1988).
Kudo S.,et al.Proc. Natl. Acad. Sci. U.S.A. 86:4619-4623(1989).
Jawad K.,et al.Nucleic Acids Res. 18:5829-5836(1990).
Kudo S.,et al.J. Biochem. 116:183-192(1994).
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