Anti-DEP1/PTPRJ Antibody Picoband® Fluoro488 Conjugated

Receptor-type tyrosine-protein phosphatase eta is an enzyme that in humans is encoded by the PTPRJ gene. The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes, including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region containing five fibronectin type III repeats, a single transmembrane region, and a single intracytoplasmic catalytic domain, and thus represents a receptor-type PTP. This protein is present in all hematopoietic lineages, and was shown to negatively regulate T cell receptor signaling possibly through interfering with the phosphorylation of Phospholipase C Gamma 1 and Linker for Activation of T Cells. This protein can also dephosphorylate the PDGF beta receptor, and may be involved in UV-induced signal transduction. Multiple transcript variants encoding different isoforms have been found for this gene.

May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca (2+) -dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca (2+) -independent manner; these are neurexins, syntaxin and AP2. Plays a role in dendrite formation by melanocytes (PubMed:23999003) .

1. Honda, H., Inazawa, J., Nishida, J., Yazaki, Y., Hirai, H. Molecular cloning, characterization, and chromosomal localization of a novel protein-tyrosine phosphatase, HPTP eta. Blood 84: 4186-4194, 1994. 2. Lesueur, F., Pharoah, P. D., Laing, S., Ahmed, S., Jordan, C., Smith, P. L., Luben, R., Wareham, N. J., Easton, D. F., Dunning, A. M., Ponder, B. A. J. Allelic association of the human homologue of the mouse modifier Ptprj with breast cancer. Hum. Molec. Genet. 14: 2349-2356, 2005. 3. Li, Y., Haarhuis, J. H. I., Sedeno Cacciatore, A., Oldenkamp, R., van Ruiten, M. S., Willems, L., Teunissen, H., Muir, K. W., de Wit, E., Rowland, B. D., Panne, D. The structural basis for cohesin-CTCF-anchored loops. Nature 578: 472-476, 2020.