Recombinant Proteins
Product List
GYPA Human
Glycophorin A Human Recombinant
GYPA Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 81 amino acids (20-91a.a.) and having a molecular mass of 9.1kDa. (Molecular size on SDS-PAGE under reducing conditions 18-28kDa).
GYPA is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
GYPC Human
Glycophorin C Human Recombinant
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.
Sf9, Baculovirus cells.
ICOSLG Human
Inducible T-Cell Costimulator Ligand Human Recombinant
ICOSLG produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 480 amino acids (19-256a.a.) and having a molecular mass of 53.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).
ICOSLG is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
Introduction
Glycophorins are a family of sialoglycoproteins found in the membrane of red blood cells (RBCs). They are classified into several types, including Glycophorin A (GPA), Glycophorin B (GPB), Glycophorin C (GPC), and Glycophorin D (GPD). These proteins are characterized by their high content of sialic acid, which contributes to the negative charge on the surface of RBCs.
Key Biological Properties: Glycophorins are integral membrane proteins that span the lipid bilayer of RBCs. They are heavily glycosylated, with carbohydrate chains that extend into the extracellular space.
Expression Patterns: Glycophorins are predominantly expressed in erythroid cells, which are precursors to mature RBCs.
Tissue Distribution: While primarily found in RBCs, glycophorins can also be detected in erythroid progenitor cells in the bone marrow.
Primary Biological Functions: Glycophorins play a crucial role in maintaining the structural integrity and flexibility of RBCs. They also contribute to the negative surface charge, which prevents RBCs from clumping together.
Role in Immune Responses: Glycophorins are involved in immune responses by acting as receptors for various pathogens, including the malaria parasite Plasmodium falciparum.
Pathogen Recognition: The carbohydrate chains on glycophorins serve as binding sites for pathogens, facilitating their entry into RBCs.
Mechanisms with Other Molecules and Cells: Glycophorins interact with other membrane proteins and cytoskeletal components to maintain RBC shape and stability.
Binding Partners: Glycophorins bind to various molecules, including lectins, antibodies, and pathogens.
Downstream Signaling Cascades: Upon binding to pathogens or antibodies, glycophorins can initiate signaling cascades that lead to cellular responses, such as phagocytosis or immune activation.
Regulatory Mechanisms: The expression and activity of glycophorins are tightly regulated at multiple levels.
Transcriptional Regulation: The genes encoding glycophorins are regulated by transcription factors that control their expression during erythropoiesis.
Post-Translational Modifications: Glycophorins undergo various post-translational modifications, including glycosylation and phosphorylation, which affect their function and interactions.
Biomedical Research: Glycophorins are used as markers for erythroid cells in research studies. They are also studied for their role in malaria infection and other diseases.
Diagnostic Tools: Antibodies against glycophorins are used in blood typing and compatibility testing.
Therapeutic Strategies: Targeting glycophorin-pathogen interactions is being explored as a potential therapeutic strategy for preventing malaria and other infections.
Development: Glycophorins are essential for the proper development of RBCs during erythropoiesis.
Aging: The expression and function of glycophorins can change with age, affecting RBC lifespan and function.
Disease: Alterations in glycophorin expression or function are associated with various diseases, including hereditary spherocytosis, malaria, and certain types of anemia.
