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:

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

News

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.

PRL-1 (2-173) N termnal GST tag

  • Product Code: X1657E
  • Size: 10 µg
  • Price (USD): $361

Cat #

X1657E		 Quantity:      

Data Sheet

Product Name

PRL-1 (2-173) N termnal GST tag

Host/Source

E.coli

Isotype

N/A

Product Type

Active Enzyme

Reactivity

Human

Applications

Useful for the study of enzyme kinetics, regulation, to dephosphorylate target substrates and for screening inhibitors.

Size

10 µg

Price (USD)

$361

Background

The product of the PRL-1 gene (alternate gene names PTP4A1 Synonyms: DKFZp779M0721, hPTPCAAX1) is a protein tyrosine phosphatase also known as phosphatase of regenerating liver, Protein tyrosine phosphatase type IVA, member 1, PTPCAAX1 or Hypothetical protein DKFZp779M0721. Protein tyrosine phosphatases play important roles in the regulation of cell growth, development, and differentiation. PRL-1 is one of the most interesting immediate early growth response genes in regenerating liver. The gene encodes a novel 20-kDa nuclear protein tyrosine phosphatase. Other than the signature sequence for PTPases, PRL-1 is not homologous to either the dual specificity PTPases (cdc25 and MKP-1) or monospecific PTPases. PRL-1 is elevated throughout the major proliferative phase of liver regeneration when hepatocytes and nonparenchymal cells in the liver are rapidly proliferating. PR-1 is also expressed at high levels in other proliferating cells including tumor cell lines such as hepatomas. PRL-1-transfected cells showed altered growth characteristics, including a faster doubling time, growth to a greater saturation density, altered morphology, and evidence of anchorage-independent growth. Overexpression of human PRL-1 in epithelial cells results in tumor formation in nude mice.

Immunogen

Recombinant enyzme produced in E. coli

Formulation

Provided in 25 mM Tris-HCl, 75 mM NaCl, pH 8.0, 0.05% Tween, 5 mM DTT and 50% glycerol

Customer Storage

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

Target Molecular Weight

45.7 kDa

Database Links:

GenBankBC023975Human

References

[1] Cates C.A., Michael R.L., Stayrook K.R., Harvey K.A., Burke Y.D., Randall S.K., Crowell P.L., Crowell D.N.; Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases.; Cancer Lett. 110:49-55(1996).
[2] Peng Y., Genin A., Spinner N.B., Diamond R.H., Taub R.; The gene encoding human nuclear protein tyrosine phosphatase, PRL-1. Cloning, chromosomal localization, and identification of an intron enhancer.; J. Biol. Chem. 273:17286-17295(1998).
[3] Gjorloff-Wingren A, Saxena M, Han S, Wang X, Alonso A, Renedo M, Oh P, Williams S, Schnitzer J, Mustelin T. Subcellular localization of intracellular protein tyrosine phosphatases in T cells.
Eur J Immunol. 2000 Aug;30(8):2412-21.
[4] Yarovinsky TO, Rickman DW, Diamond RH, Taub R, Hageman GS, Bowes Rickman C.
Expression of the protein tyrosine phosphatase, phosphatase of regenerating liver 1, in the outer segments of primate cone photoreceptors. Brain Res Mol Brain Res. 2000 Apr 14;77(1):95-103.
[5] Carter DA. Expression of a novel rat protein tyrosine phosphatase gene. Biochim Biophys Acta. 1998 Nov 8;1442(2-3):405-8.
[6] Zeng Q, Hong W, Tan YH. Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1. Biochem Biophys Res Commun. 1998 Mar 17;244(2):421-7.
[7] Cates CA, Michael RL, Stayrook KR, Harvey KA, Burke YD, Randall SK, Crowell PL, Crowell DN Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases. Cancer Lett. 1996 Dec 20;110(1-2):49-55.
[8] Takano S, Fukuyama H, Fukumoto M, Kimura J, Xue JH, Ohashi H, Fujita J. PRL-1, a protein tyrosine phosphatase, is expressed in neurons and oligodendrocytes in the brain and induced in the cerebral cortex following transient forebrain ischemia. Brain Res Mol Brain Res. 1996 Aug;40(1):105-15.