Recombinant Proteins

p53
LBP
CEA
HLA
TCL
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NPM
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GYPA Human

Glycophorin A Human Recombinant

Recombinant human GYPA, produced in Sf9 insect cells, is a single, glycosylated polypeptide chain consisting of 81 amino acids (20-91a.a.). It has a molecular mass of 9.1 kDa. On SDS-PAGE under reducing conditions, its molecular size appears between 18-28 kDa. The protein is expressed with a 9 amino acid His tag at the C-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT11675
Source
Sf9, Insect cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

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. The molecular size on SDS-PAGE will appear at approximately 18-28kDa. GYPC is expressed with a 6 amino acid His tag at the C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11721
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

ICOSLG Human

Inducible T-Cell Costimulator Ligand Human Recombinant

Produced in Sf9 Baculovirus cells, our ICOSLG is a single, glycosylated polypeptide chain comprising 480 amino acids (19-256a.a.). It has a molecular mass of 53.7kDa, although it may appear between 50-70kDa on SDS-PAGE due to glycosylation. The protein is expressed with a C-terminal 239 amino acid hIgG-His-tag and purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT11777
Source

Sf9, Baculovirus cells.

Appearance
A clear, colorless solution that has been sterilized by filtration.
Definition and Classification

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.

Biological Properties

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.

Biological Functions

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.

Modes of Action

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

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.

Applications

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.

Role in the Life Cycle

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.

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