1. Recombinant Proteins
  2. Receptor Proteins
  3. Enzyme-linked receptors
  4. R7 RPTPs

Tyrosine phosphatase receptors (RPTPs), as known as receptor-like tyrosine phosphatasesor receptor protein tyrosine phosphatases, are a family of integral cell surface proteins that possess intracellular PTP activity and extracellular domains that have sequence homology to cell adhesion molecules. RPTPs consist of a single transmembrane spanning domain, variable N-terminal extracellular regions (ECDs) and either a single or tandem intracellular phosphatase domain. Based on sequence features of their ECDs, the RPTP family can be grouped into 8 sub-families: R1/R6; R2A; R2B; R3; R4; R5; R7; and R8. RPTPs are enzymatic and functional counterparts of RPTKs and initiate intracellular tyrosine phosphorylation-dependent signal transduction in response to binding of extracellular ligands, such as growth factors and cytokines. They are involved in various aspects of cellular functions, such as proliferation, differentiation, survival, migration, and metabolism. The type R7 RPTPs subfamily members have one cytoplasmic phosphatase domain and a short extracellular domain. This subfamily is constituted by PTPRR and STEP (striatal-enriched protein tyrosine phosphatase). PTPRR have shown to modulate the activity of some members of the mitogen-activated protein kinase (MAPK) pathway.