• Official Full Name

    protein tyrosine phosphatase, receptor type, M

  • Overview

    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 tra
  • Synonyms

    PTPRM; protein tyrosine phosphatase, receptor type, M; PTPRL1; receptor-type tyrosine-protein phosphatase mu; hR PTPu; RPTPU; protein tyrosine phosphatase mu; protein-tyrosine phosphatase mu; protein tyrosine phosphatase, receptor type, mu polypeptide; RP;

  • Recombinant Proteins
  • Protein Pre-coupled Magnetic Beads
  • Human
  • Human
  • Mouse
  • E.coli
  • HEK293
  • Mammalian Cell
  • Sf9 Insect Cell
  • GST
  • His
  • His (Fc)
  • Avi
  • His|T7
  • N/A
  • N
Species Cat.# Product name Source (Host) Tag Protein Length Price
Human PTPRM-336H Active Recombinant Human Protein Tyrosine Phosphatase, Receptor Type, M E.coli N/A
Human PTPRM-219H Active Recombinant Human PTPRM(879-1184) Protein, N-GST-tagged E.coli GST 879-1184 aa
Human PTPRM-382H Recombinant Human PTPRM, GST-tagged Sf9 Insect Cell GST
Human PTPRM-7017H Recombinant Human PTPRM , GST-tagged Sf9 Insect Cell GST 764-1452 aa
Human PTPRM-1861H Recombinant Human PTPRM, GST-tagged E.coli GST
Human PTPRM-5628H Recombinant Human PTPRM protein, His & T7-tagged E.coli His/T7 Thr1197~Ser1403 (Accession # P28827)
Human PTPRM-2384H Recombinant Human PTPRM, GST-tagged E.coli GST
Human PTPRM-5469H Recombinant Human Protein Tyrosine Phosphatase, Receptor Type, M E.coli N/A
Human PTPRM-6108H Recombinant Human PTPRM Protein (Thr1197-Ser1403), N-His tagged E.coli N-His Thr1197-Ser1403
Mouse PTPRM-13701M Recombinant Mouse PTPRM Protein Mammalian Cell His
Mouse PTPRM-7288M Recombinant Mouse PTPRM Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Mouse PTPRM-7288M-B Recombinant Mouse PTPRM Protein Pre-coupled Magnetic Beads HEK293
  • Involved Pathway
  • Protein Function
  • Interacting Protein
  • Other Resource

PTPRM involved in several pathways and played different roles in them. We selected most pathways PTPRM participated on our site, such as Cell adhesion molecules (CAMs), Adherens junction, which may be useful for your reference. Also, other proteins which involved in the same pathway with PTPRM were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

Pathway Name Pathway Related Protein
Cell adhesion molecules (CAMs)HLA-DRB5;NRCAM;ITGA6B;CLDN15;SDC1;NADL1.2;LRRC4C;JAM2A;SDC3

PTPRM has several biochemical functions, for example, cadherin binding, identical protein binding, protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by PTPRM itself. We selected most functions PTPRM had, and list some proteins which have the same functions with PTPRM. You can find most of the proteins on our site.

Function Related Protein
identical protein bindingMVK;CPT1A;ESYT2;LYZ1;SOX10;DPP4;TRIP13;SNCAIP;CLDN9
protein bindingBUD13;URI1;MED17;INPP5D;ACAT2;CARD8;EFHC2;DDX47;JAG1
protein tyrosine phosphatase activityEYA4;DUSP12;MDP1;SSH2;PTPN11;PTPN22;PTPN13;MTMR3;PTPN6
transmembrane receptor protein tyrosine phosphatase activityPTPRD;PTPRN2;PTPRR;PTPRUB;PTPRA;PTPRS;PTPN6;PTPRM;PTPRO

PTPRM has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with PTPRM here. Most of them are supplied by our site. Hope this information will be useful for your research of PTPRM.

LCK; Cdh1; Cdh2; Cdh4; nagA

Gene Family


Research Area

Related articles

Luckerath, K; Kirkin, V; et al. Immune modulation by Fas ligand reverse signaling: lymphocyte proliferation is attenuated by the intracellular Fas ligand domain. BLOOD 117:519-529(2011).
Charba, DS; Wiggins, RC; et al. Antibodies to protein tyrosine phosphatase receptor type O (PTPro) increase glomerular albumin permeability (P(alb)). AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY 297:F138-F144(2009).
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