Cell Signaling Technology

Product Pathways - Phosphatases

PTPmu (BK2) Mouse mAb #4485

Applications Reactivity MW (kDa) Source Isotype
W IP H R Mi (M) 100, 110, 210 Mouse IgG2a

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mi=Mink
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

PTPmu Mouse mAb detects endogenous levels of total PTPmu protein. This antibody does not cross react with other receptor tyrosine phosphatases.

Source / Purification

Monoclonal antibody (isotype: IgG2a) is produced by immunizing mice with a synthetic peptide (KLH-coupled) corresponding to the amino-terminal residues of human PTPmu.

Western Blotting

Western Blotting

Western blot analysis of extract from MvLu cells using PTPmu (BK2) Mouse mAb.

Background

Receptor tyrosine phosphatase PTPmu has an extracellular segment characteristic of adhesion molecules: an MEM domain, an Ig domain and four fibronectin III like (FN III) repeats (1,2). PTPmu is proteolytically cleaved into two noncovalently associated fragments: one is the extracellular domain, the other includes the transmembrane and the intracellular catalytic domains. Both fragments are approximately 100 kDa (3). The extracellular domain mediates cell-cell adhesion in a homophilic, Ca2+ independent manner (1,2). PTPmu associates with multiple cadherins (4). It is able to restore E-cadherin-dependent adhesion in human prostate cancer, and is required for N-cadherin-mediated neurite outgrowth (5,6). The phosphatase activity seems to be essential for the latter function but is dispensable for the former (5,6). PTPmu also associates with and recruits a scaffold protein, RACK (receptor for activated protein C kinase), to cell-cell contact sites (7). Both PKCdelta and src seem to be involved in this process (6,7).

  1. Gebbink, M. F. et al. (1993) J. Biol. Chem. 268, 16101-16104.
  2. Brady-Kalnay, S.M. and Tonks, N.K. (1994) J. Biol. Chem. 269, 28472-28477.
  3. Brady-Kalnay, S. M. et al. (1998) J. Cell Biol. 141, 287-296.
  4. Hellberg, C. B. et al. (2002) J. Biol. Chem. 277, 11165-11173.
  5. Burden-Gulley, S.M. and Brady-Kalnay, S.M. (1999) J. Cell Biol. 144, 1323-1336.
  6. Mourton, T. et al. (2001) J. Biol. Chem. 276, 14896-14901.

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