GYPC Human
Sf9, Baculovirus cells.
Glycophorin C (Gerbich Blood Group), Sialoglycoprotein D, Glycoprotein Beta, Glycoconnectin, Glycophorin-D, PAS-2, GPD 3 4, GPC, Glycophorin-C, CD236 Antigen, CD236R, CD236, GYPD, GLPC, GE, Glycophorin-C, Glycoconnectin, Glycophorin-D, GPD, Glycoprotein beta, PAS-2', Sialoglycoprotein D.
Greater than 95.0% as determined by SDS-PAGE.
Description
GYPC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 66 amino acids (1-57a.a.) and having a molecular mass of 7.2kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). GYPC is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Glycophorin C (Gerbich Blood Group), Sialoglycoprotein D, Glycoprotein Beta, Glycoconnectin, Glycophorin-D, PAS-2, GPD 3 4, GPC, Glycophorin-C, CD236 Antigen, CD236R, CD236, GYPD, GLPC, GE, Glycophorin-C, Glycoconnectin, Glycophorin-D, GPD, Glycoprotein beta, PAS-2', Sialoglycoprotein D.
Sf9, Baculovirus cells.
ADPMWSTRSP NSTAWPLSLE PDPGMASAST TMHTTTIAEP DPGMSGWPDG RMETSTPTIM HHHHHH.
Product Science Overview
Glycophorin C (GPC) is a minor sialoglycoprotein found in the membranes of human erythrocytes (red blood cells). It plays a crucial role in maintaining the stability and shape of red blood cells and serves as a receptor for the malaria parasite, Plasmodium falciparum . The recombinant form of Glycophorin C is produced using various expression systems, such as baculovirus-infected insect cells, to study its structure and function in detail .
The Glycophorin C antigen was first discovered in 1960 when three women who lacked the antigen developed anti-Gea antibodies during pregnancy. The antigen was named after one of the patients, Mrs. Gerbich . Subsequent research identified additional related antigens, leading to the classification of the Gerbich blood group system .
Glycophorin C is encoded by the GYPC gene located on chromosome 2 (2q14-q21). The gene consists of four exons that encode a single polypeptide chain of 128 amino acids . The protein is organized into three domains:
- Extracellular Domain: Encoded by exons 1, 2, and part of exon 3, this domain contains the binding sites for the malaria parasite and the Gerbich antigens.
- Transmembrane Domain: Encoded by the remainder of exon 3 and part of exon 4, this domain anchors the protein in the erythrocyte membrane.
- Cytoplasmic Domain: Encoded by the remainder of exon 4, this domain interacts with the cytoskeleton of the erythrocyte, contributing to cell shape and stability .
Recombinant Glycophorin C is typically produced using baculovirus-infected insect cells. This method allows for high levels of protein expression and proper post-translational modifications, such as glycosylation . The recombinant protein is often tagged with a His tag to facilitate purification and is characterized by its high purity (>95%) and low endotoxin levels (<1 EU/µg) .
Glycophorin C plays a vital role in the structural integrity of red blood cells. It interacts with protein 4.1, a cytoskeletal protein, to maintain the biconcave shape of erythrocytes . Additionally, Glycophorin C serves as a receptor for the Plasmodium falciparum merozoites, making it a target for malaria research .
Recombinant Glycophorin C is used in various research applications, including:
- Structural Studies: Understanding the protein’s structure and its interactions with other molecules.
- Malaria Research: Investigating the binding mechanisms of Plasmodium falciparum and developing potential therapeutic interventions.
- Blood Group Studies: Exploring the genetic variations and clinical significance of the Gerbich blood group system .
