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.

PTP1B (1-321)/PTPN1

  • Product Code: X1659E
  • Size: 20 µg
  • Price (USD): $361

Cat #

X1659E		 Quantity:      

Data Sheet

Product Name

PTP1B (1-321)/PTPN1


Protein Tyrosine Phosphatase 1B



Product Type

Active Enzyme




Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.


20 µg

Price (USD)



Tyrosine-protein phosphatase, non-receptor type 1 (PTP1B) also know as Protein-tyrosine phosphatase 1B, PTPN1 is a PTP (protein tyrosine phosphatase) first isolated from human placenta. The protein is unrelated to other known phosphatases but is similar to common leukocyte antigen (CD45) and to LAR a homolog of the neural adhesion molecule NCAM. PTP1B negatively regulates insulin sensitivity by dephosphorylating the insulin receptor. Akt is a ser/thr kinase effector of insulin signaling that phosphorylates substrates at the consensus motif RXRXXS/T. PTP1B contains the Akt phosphorylation motif (RYRDVS50), and PTP1B (but not mutants with substitutions for Ser50) are phosphorylated by Akt. Insulin stimulation also causes a significant increase in phosphorylation of PTP1B.


Recombinant enyzme produced in E. coli


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

63.3 kDa

Database Links:



[1] Chernoff J., Schievella A.R., Jost C.A., Erikson R.L., Neel B.G.; Cloning of a cDNA for a major human protein-tyrosine-phosphatase.; Proc. Natl. Acad. Sci. U.S.A. 87:2735-2739(1990).
[2] Brown-Shimer S., Johnson K.A., Lawrence J.B., Johnson C., Bruskin A., Green N.R., Hill D.E.;
Molecular cloning and chromosome mapping of the human gene encoding protein phosphotyrosyl phosphatase 1B.; Proc. Natl. Acad. Sci. U.S.A. 87:5148-5152(1990).
[3] Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., , Rogers J.; The DNA sequence and comparative analysis of human chromosome 20.; Nature 414:865-871(2001).
[4] Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., , Marra M.A.;
Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.; Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
[5] Charbonneau H., Tonks N.K., Kumar S., Diltz C.D., Harrylock M., Cool D.E., Krebs E.G., Fischer E.H., Walsh K.A.; Human placenta protein-tyrosine-phosphatase: amino acid sequence and relationship to a family of receptor-like proteins.; Proc. Natl. Acad. Sci. U.S.A. 86:5252-5256(1989).
[6] Flint A.J., Gebbink M.F.G.B., Franza B.R. Jr., Hill D.E., Tonks N.T.; Multi-site phosphorylation of the protein tyrosine phosphatase, PTP1B: identification of cell cycle regulated and phorbol ester stimulated sites of phosphorylation.; EMBO J. 12:1937-1946(1993).
[7] Frangioni J.V., Beahm P.H., Shifrin V., Jost C.A., Neel B.G.; The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence.; Cell 68:545-560(1992).
[8] Ravichandran L.V., Chen H., Li Y., Quon M.J.; Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor.; Mol. Endocrinol. 15:1768-1780(2001).
[9] Barford D., Flint A.J., Tonks N.K.; Crystal structure of human protein tyrosine phosphatase 1B.;
Science 263:1397-1404(1994).
[10] Puius Y.A., Zhao Y., Sullivan M., Lawrence D.S., Almo S.C., Zhang Z.Y.; Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design.; Proc. Natl. Acad. Sci. U.S.A. 94:13420-13425(1997).
[11] Pannifer A.D., Flint A.J., Tonks N.K., Barford D.; Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by X-ray crystallography.; J. Biol. Chem. 273:10454-10462(1998).
[12] Groves M.R., Yao Z.-J., Roller P.P., Burke T.R. Jr., Barford D.; Structural basis for inhibition of the protein tyrosine phosphatase 1B by phosphotyrosine peptide mimetics.; Biochemistry 37:17773-17783(1998).