GYPA Human

Glycophorin A (GPA) is a significant sialoglycoprotein found in the membrane of human erythrocytes (red blood cells). It plays a crucial role in maintaining the structural integrity and functionality of red blood cells. The recombinant form of Glycophorin A is produced using advanced biotechnological methods, allowing for its use in various research and clinical applications.

Glycophorin A is a transmembrane protein composed of 131 amino acids. The recombinant human Glycophorin A protein typically includes a sequence from Met1 to Glu91, expressed with a C-terminal polyhistidine tag for purification purposes . The recombinant protein is produced in HEK293 cells, ensuring proper post-translational modifications such as glycosylation, which is essential for its biological activity .

The recombinant human Glycophorin A comprises 83 amino acids and has a predicted molecular mass of 9.4 kDa. However, due to glycosylation, the apparent molecular mass of the protein is approximately 35-45 kDa and 20 kDa in SDS-PAGE under reducing conditions . This glycosylation is crucial for the protein’s stability and function.

Glycophorin A is involved in various biological processes, including:

• Cell-Cell Interactions: It mediates interactions between red blood cells and other cells, playing a role in cell adhesion.
• Pathogen Binding: GPA serves as a receptor for certain pathogens, including the malaria parasite Plasmodium falciparum, facilitating their entry into red blood cells.
• Blood Group Antigen: It carries the MN blood group antigens, which are important for blood transfusion compatibility.

Recombinant Glycophorin A is used in several research and clinical applications:

• Immunoassays: It is used as a standard or control in various immunoassays to study red blood cell antigens.
• Vaccine Development: GPA is explored as a target for vaccine development against malaria and other infectious diseases.
• Drug Discovery: It is used in drug screening assays to identify compounds that can inhibit pathogen binding to red blood cells.

The production of recombinant Glycophorin A involves the expression of the GPA gene in HEK293 cells. The protein is then purified using affinity chromatography, leveraging the polyhistidine tag for efficient purification . The final product is lyophilized from sterile PBS, pH 7.4, and typically contains protectants such as trehalose, mannitol, and Tween80 to ensure stability during storage .

Recombinant Glycophorin A is stable for up to twelve months when stored at -20°C to -80°C under sterile conditions. It is recommended to aliquot the protein to avoid repeated freeze-thaw cycles, which can degrade the protein .