Human Glycophorin-C (GYPC) Protein
234€ (2 µg)
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Name
Human Glycophorin-C (GYPC) Protein
Category
Proteins and Peptides
Provider
Abbexa
Reference
abx680114
Tested Applications
SDS-PAGE
Description
Human Glycophorin-C (GYPC) Protein is a recombinant protein produced in Sf9, Baculovirus cells.
Documentos del producto
Instrucciones
Data sheet
Especificaciones del producto
| Category | Proteins and Peptides |
| Immunogen Target | Glycophorin-C (GYPC) |
| Host | Insect |
| Origin | Human |
| Conjugation | Unconjugated |
| Expression | Recombinant |
| Purity | > 95% (SDS-PAGE) |
| Size 1 | 2 µg |
| Size 2 | 10 µg |
| Size 3 | 1 mg |
| Form | Liquid |
| Tested Applications | SDS-PAGE |
| Availability | Shipped within 5-10 working days. |
| Dry Ice | No |
| Alias | Gerbich blood group,GE,GPC,GPD,GYPD,CD236,PAS-2,CD236R,Glycoconnectin,Glycophorin-D,Glycoprotein beta, |
| Background | Protein GYPC |
| Status | RUO |
| Note | THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION. |
Background
Glycophorin C (GYPC) is a membrane glycoprotein found primarily on the surface of red blood cells (RBCs). It is a member of the glycophorin family, which includes Glycophorin A (GYPA) and Glycophorin B (GYPB). GYPC plays a crucial role in maintaining the structural integrity of the RBC membrane and contributes to the MNS blood group system. The protein is encoded by the GYPC gene located on chromosome 2. Along with its homologs GYPA and GYPB, GYPC is involved in defining RBC membrane characteristics, including cell shape, flexibility, and interactions with the cytoskeleton. GYPC, specifically, is known to carry the M and N antigens of the MNS blood group system, which are significant in transfusion medicine. In addition to its structural function in the RBC membrane, GYPC plays a role in the function of the erythrocyte by interacting with various signaling molecules and maintaining the membrane's elasticity and resistance to mechanical stresses. Its functional importance in RBCs, as well as its potential relevance in certain disease states, makes it a significant protein in both clinical and biological research.
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