Monoclonal antibodies 3G4 and 3D7 have been directed against the extracellular domain of RPTPμ.
Purification
Purified
Immunogen
This antibody has been derived by fusion of SP2/0 mouse myeloma cells with spleen cells from a BALB/c mouse immunized with ExG protein, secreted by NIH-3T3 transfected cells and purified with glutahione beads. The cells have been transfected using a fusion construct, termed ExG, encoding the entire ectodomain of the Human RPTPmu molecule (aa 1-742), fused COOH terminally to GST.
RPTPrho antibody, RPTP-rfo antibody, mKIAA0283 antibody, protein tyrosine phosphatase, receptor type T antibody, protein tyrosine phosphatase, receptor type, T antibody, PTPRT antibody, Ptprt antibody
Background
Receptor-like protein tyrosine phosphatases (RPTPs) represent a new family of transmembrane proteins that are thought to transduce external signals by dephosphorylating phosphotyrosine residues on intracellular substrates. RPTPμ is a prototypic receptor-like protein-tyrosine phosphatase (RPTP) that mediates homotypic cell-cell interactions. Intracellularly, RPTPμ consists of a relatively large juxtamembrane region (about 150 amino acids) and two conserved phosphatase domains. As in most RPTPs, the first (membrane-proximal) PTP domain of RPTPμ is catalytically active, whereas its second (C-terminal) domain is inactive. RPTPμ is involved in cell-cell adhesion through homophilic interactions and may also play a key role in signal transduction and growth control.