PTPRM Antibody – Goat Polyclonal

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, a single transmembrane region, and two tandem catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP mu (MAM) domain, an Ig-like domain and four fibronectin type III-like repeats. This PTP has been shown to mediate cell-cell aggregation through the interaction with another molecule of this PTP on an adjacent cell. This PTP can interact with scaffolding protein RACK1/GNB2L1, which may be necessary for the downstream signaling in response to cell-cell adhesion. Alternative splicing results in multiple transcripts encoding distinct isoforms. [provided by RefSeq, Jul 2008]

PTPRM: a single-pass type I membrane protein involved in cell-cell adhesion through homophilic interactions. A protein-tyrosine phosphatase receptor of the class 2B subfamily. A negative regulator of proliferation and invasion of breast cancer cells. The PTPRM gene is frequently hypermethylated in sporadic cancers. Modulates p120 catenin phosphorylation, promoting adipogenic differentiation. Two isoforms of the human protein have been reported.

Protein type: EC 3.1.3.48; Membrane protein, integral; Motility/polarity/chemotaxis; Phosphatase; Receptor protein phosphatase, tyrosine

Chromosomal Location of Human Ortholog: 18p11.23

Cellular Component: cell-cell adherens junction; cytoplasm; intercellular junction; lamellipodium; perinuclear region of cytoplasm

Molecular Function: cadherin binding; identical protein binding; protein binding; protein tyrosine phosphatase activity; transmembrane receptor protein tyrosine phosphatase activity

Biological Process: homophilic cell adhesion; negative regulation of angiogenesis; negative regulation of endothelial cell proliferation; neurite development; protein amino acid dephosphorylation; response to drug; retinal ganglion cell axon guidance; signal transduction