1. Recombinant Proteins
  2. Receptor Proteins
  3. Enzyme-linked receptors
  4. R2B 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 R2B RPTPs subfamily members display a single immunoglobulin-like (Ig) domain, multiple fibronectin type III domains (FNIII), and a meprin-A5-PTP µ (MAM) domains in their ECDs. A representative R2B subfamily member is RPTP-κ, which is encoded by the Ptprk gene.