PDGFR
Platelet-derived growth factor receptors (PDGFRs) belong to the receptor tyrosine kinase (RTK) family and serve the function of protein tyrosine kinases. PDGFRs are activated by binding to their ligand PDGFs, and involved in a variety of cellular processes, e.g. proliferation, migration, survival, and cancer development. PDGFRs are primarily located in vascular endothelial cells, fibroblasts and Kupffer cells. The two types of receptor, PDGFR-α and PDGFR-β, are structurally similar and consist of extracellular domains with five immunoglobulin (Ig) - like domains and intracellular parts with kinase domains which contain characteristic inserts of about 100 amino acid residues without homology to kinases. Ligand binding occurs mainly to Ig-like domains 2 and 3, and causes dimerization of the receptors, which is further stabilized by direct receptor-receptor interactions involving Ig-like domain 4.The dimerization is a key event in activation since it juxtaposes the intracellular parts promoting autophosphorylation in trans between the receptors. Subsequently, the phosphorylated PDGFR can initiate various downstream signaling events by recruiting SH2 domain-containing molecules such as Src kinase, Grb2, SHP2, PLCγ, Nck, and STAT.
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PDGFR Recombinant Proteins (22)
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Inhibitors & Agonists (308)
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Recombinant Protein Expression Service
- Codon Optimization
- Gene Synthesis
- Construction of Expression Vector
- Strain Screening
- Protein Expression
- Purification & QC
- Protein Delivery
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- Formula: Human
- Molecular Weight: Sf9 insect cells
The EpCAM/TROP1 protein serves as an important homogeneous interacting molecule that promotes direct contact between intestinal epithelial cells (IEC) and intraepithelial lymphocytes (IEL) in the mucosal epithelium. This feature helps establish an immune barrier against mucosal infections. EpCAM/TROP1 Protein, Human (His-SUMO) is the recombinant human-derived EpCAM/TROP1 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag.
