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PTP1B drug discovery kit

BML-AK822-0001 96 wells 479.00 USD
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The PTP1B Tyrosine Phosphatase Drug Discovery Kit is a colorimetric, non-radioactive assay designed to measure the phosphatase activity of purified PTP1B. This 96-well assay is useful for screening inhibitors and modulators of PTP1B activity.The kit includes human, recombinant PTP1B (residues 1-322; MW=37.4 kDa), expressed in E. coli. The detection of free phosphate released is based on the classic Malachite green assay and offers the advantages of convenient, 1-step detection and excellent sensitivity, without radioactivity. PTP1B (protein tyrosine phosphatase-1B) is a ubiquitous, nontransmembrane protein tyrosine phosphatase, originally identified in human placenta.

It is implicated in the negative regulation of insulin receptor signaling, and is a potential therapeutic target for treatment of type 2 diabetes and obesity. The phosphopeptide substrate supplied with this kit ("IR5", Prod. No. BML-P315, pTyr1158 (a.k.a. pTyr1146, mature peptide numbering)) contains sequence from the insulin receptor β subunit domain that must be autophosphorylated to achieve full receptor kinase activation. This "activation loop" is the target of several protein phosphatase regulators of insulin signaling, including, notably, PTP1B. The PTP1B inhibitor suramin is supplied as a control for inhibitor detection. Suramin is a reversible and competitive inhibitor of PTP1B, with a Ki of 5.5 µM.

Product Specification

Applications:Colorimetric detection, HTS
Use/Stability:Store all components except the microtiter plate at -70°C for the highest stability. The PTP1B enzyme component BML-SE332-9092 must be handled particularly carefully in order to retain maximal enzymatic activity. Thaw it quickly in a RT water bath or by rubbing between fingers, then immediately store on an ice bath. The remaining unused enzyme should be 'snap' frozen, e.g. in liquid nitrogen or a dryice/ethanol bath, and stored at -70°C. If only a few assays are to be performed each day, the PTP1B may be divided into several aliquots (best if ≥%10 µl)) to help minimize freeze/thaw cycles.
Shipping:Shipped on Dry Ice
Long Term Storage:-80°C
Kit/Set Contains:PTP 1B Enzyme, Substrate (“IR5” Insulin Receptor β, residues 1142-1153, pY1146), Assay Buffer, Biomol Red™ Concentrated Phosphate Detection Reagent, Suramin (PTP1B inhibitor), Phosphate Standard, and Microplate (½-volume)
UniProt ID:P18031

Product Literature References

Novel Imbricatolic acid derivatives as protein tyrosine phosphatase-1B inhibitors: Design, synthesis, biological evaluation and molecular docking: M.F. Khan, et al.; Bioorg. Med. Chem. Lett. 26, 1988 (2016), Application(s): Evaluation of PTP-1B inhibitory activity of C20H34O3 and its derivatives, Abstract;
Optimization of extraction parameters of PTP1β (protein tyrosine phosphatase 1β), inhibitory polyphenols, and anthocyanins from Zea mays L. using response surface methodology (RSM): S.H. Hwang, et al.; BMC Complement. Altern. Med. 16, 317 (2016), Application(s): Enzymatic assay measurement of PTP1β inhibitory activity, Abstract; Full Text
In vitro cytotoxic, in vitro and in vivo antidiabetic activity of roylea cineria: R.P. Bahuguna, et al.; Sci. Revs. Chem. Commun. 5, 69 (2015), Application(s): Assay using plant fractions, Full Text

General Literature References

Protein-tyrosine phosphatase 1B deficiency reduces insulin resistance and the diabetic phenotype in mice with polygenic insulin resistance: B. Xue et al.; J. Biol. Chem. 282, 23829 (2007), Abstract;
SIRT1 improves insulin sensitivity under insulin-resistant conditions by repressing PTP1B: C. Sun et al.; Cell. Metab. 6, 307 (2007), Abstract;
Suramin derivatives as inhibitors and activators of protein-tyrosine phosphatases: D.F. McCain et al.; J. Biol. Chem 279, 14713 (2004), Abstract;
Mechanism of transmembrane signaling: insulin binding and the insulin receptor: F.P. Ottensmeyer et al.; Biochemistry 39, 12103 (2000), Abstract;
Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B: A. Salmeen et al.; Mol. Cell. 6, 1401 (2000), Abstract;
Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene: M. Elchbly et al.; Science 283, 1544 (1999), Abstract;
Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog: S.R. Hubbard; Embo. J. 16, 5572 (1997), Abstract;
Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design: Y.A. Pius et al.; PNAS 94, 13420 (1997), Abstract;
Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src homology 3 domain of p130(Cas): F. Liu et al.; J. Biol. Chem. 271, 31290 (1996), Abstract;
Characterization and kinetic analysis of the intracellular domain of human protein tyrosine phosphatase beta (HPTP beta) using synthetic phosphopeptides: K.W. Harder et al.; Biochem. J. 298, 395 (1994), Abstract;
Sequential dephosphorylation of a multiply phosphorylated insulin receptor peptide by protein tyrosine phosphatases: C. Ramachandran et al.; Biochemistry 31, 4232 (1992), Abstract;
Use of fluorinated tyrosine phosphates to probe the substrate specificity of the low molecular weight phosphatase activity of calcineurin: B. Martin et al.; J. Biol. Chem. 260, 14932 (1985), Abstract;

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