Exalpha Biologicals, Inc.

Accelerating the Pace of Discovery

Product Highlight

Mouse anti-M13 phage coat protein g8p

Antibodies recognising M13 filamentous phage coat proteins are instrumental in the selection and detection of phages expressing specific antibody fragments or peptide sequences at their surface. The monoclonal antibodies manufactured and supplied by Exalpha react with either the pIII (g3p) or pVIII (g8p) proteins of M13 filamentous bacteriophage. All antibodies are available in a purified format. The antibodies are fully validated and are suitable for a wide range of techniques including:

  • Flow Cytometry
  • Western Blot
  • Immunohistochemistry
  • Immunoprecipitation
For more information, click here for our M13 Bacteriophage information page.


Two more of our excellent products have been published by PubMed:

Potential actionable targets in appendiceal cancer detected by immunohistochemistry, fluorescent in situ hybridization, and mutational analysis
Borazanci, E., et al., J. Gastrointest. Oncol., 8, 164-172 (2017)
Using Exalpha SPARC Antibody (Cat. No. X1867P)

Molecular mechanism underlying the pharmacological interactions of the protein kinase C-β inhibitor enzastaurin and erlotinib in non-small cell lung cancer cells
Steen, N.V., et al., Am. J. Cancer Res., 7, 816-830 (2017)
Using Exalpha's FITC labeled anti PY20 Antibody (Cat. No. X1017)

Exalpha Biologicals, Inc.

RPTPgamma (801-1147) N Terminal GSTS Tag

  • Product Code: X1666E
  • Size: 20 µg
  • Price (USD): $361

Cat #

X1666E		 Quantity:      

Data Sheet

Product Name

RPTPgamma (801-1147) N Terminal GSTS Tag



Product Type

Active Enzyme




Study of enzyme kinetics, regulation and to dephosphorylate target substances


20 µg

Price (USD)



RPTP gamma, also known as Receptor-type tyrosine-protein phosphatase gamma, R-PTP-gamma or PTPRG is a protein tyrosine phosphatase (PTP) is a candidate tumor suppressor gene since it is located on human chromosome 3p14.2-p21, a region frequently deleted in certain types of renal and lung carcinomas. In situ hybridization analysis reveals that RPTP gamma mRNA is expressed in specific regions of the brain and that the localization of RPTP gamma changes during brain development. RPTP gamma is composed of a putative extracellular domain, a single transmembrane domain, and a cytoplasmic portion with two tandem catalytic tyrosine phosphatase domains. The extracellular domain contains a stretch of 266 amino acids with striking homology to the zinc-containing enzyme carbonic anhydrase (CAH), indicating that RPTP gamma and RPTP beta (HPTP zeta) represent a subfamily of receptor tyrosine phosphatases. RPTP gamma may have a function other than catalysis of hydration of metabolic CO2.


Recombinant enyzme produced in E. coli


Provided in 25 mM Tris-HCl, pH 8.0, 75 mM NaCl, 0.05% Tween-20, 50% glycerol, 2 mM EDTA, 1 mM DTT, 10 mM glutathione.

Customer Storage

Enzyme should be stored at -20°C. Enzyme should be kept on ice when dispensing

Target Molecular Weight

65.6 kDa

Database Links:



1: Yuki T, Ishihara S, Rumi M, Ortega-Cava Cesar F, Kadowaki Y, Kazumori H, Yuki M, Wada T, Miyaoka Y, Yoshino N, Kinoshita Y. Expression of midkine and receptor-like protein tyrosine phosphatase (RPTP)-beta genes in the rat stomach and the influence of rebamipide.
Aliment Pharmacol Ther. 2003 Jul;18 Suppl 1:106-12.

2: Robles Y, Vivas-Mejia PE, Ortiz-Zuazaga HG, Felix J, Ramos X, Pena de Ortiz S.
Hippocampal gene expression profiling in spatial discrimination learning. Neurobiol Learn Mem. 2003 Jul;80(1):80-95.

3: Hirayama T. Protein tyrosine phosphatase beta, a receptor for Helicobacter pylori vacA toxin.
Keio J Med. 2002 Dec;51 Suppl 2:20-3. Review.

4: Shintani T, Maeda N, Noda M. Receptor-like protein tyrosine phosphatase gamma (RPTPgamma), but not PTPzeta/RPTPbeta, inhibits nerve-growth-factor-induced neurite outgrowth in PC12D cells.
Dev Neurosci. 2001;23(1):55-69.

5: Chilton JK, Stoker AW. Expression of receptor protein tyrosine phosphatases in embryonic chick spinal cord. Mol Cell Neurosci. 2000 Oct;16(4):470-80.

6: Barnea G., Silvennoinen O., Shaanan B., Honegger A.M., Canoll P.D., D'Eustachio P., Morse B., Levy J.B., Laforgia S., Huebner K., Musacchio J.M., Sap J., Schlessinger J.;
Identification of a carbonic anhydrase-like domain in the extracellular region of RPTP gamma defines a new subfamily of receptor tyrosine phosphatases.; Mol. Cell. Biol. 13:1497-1506(1993).

7: Kastury K., Ohta M., Lasota J., Moir D., Dorman T., Laforgia S., Druck T., Huebner K.;
Structure of the human receptor tyrosine phosphatase gamma gene (PTPRG) and relation to the familial RCC t(3;8) chromosome translocation.; Genomics 32:225-235(1996).

8: Krueger N.X., Streuli M., Saito H.; Structural diversity and evolution of human receptor-like protein tyrosine phosphatases.;

9: Kaplan R., Morse B., Huebner K., Croce C., Howk R., Ravera M., Ricca G., Jaye M., Schlessinger J.; Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain.;
Proc. Natl. Acad. Sci. U.S.A. 87:7000-7004(1990).