SensoLyte® Green PIN1 Activity Assay Kit Fluorimetric - 1 kit
- Cat.Number : AS-72240
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Peptidyl-prolyl isomerase (PPIase) Pin1 catalyzes cis/trans isomerization of the phospho- Serine/Threonine-Proline peptide bonds. Pin1 consists of short N-terminal protein-protein interaction domain that allows enzyme to bind phosphoproteins and longer C-terminal izomerase domain. Pin1 has many biological substrates, plays critical role in cell-cycle regulation, and up-regulated in many human cancers. Recently, Pin1 was linked to the Alzheimer’s disease pathogenesis. Pin1 can bind phosphorylated Thr-212/231 residues of Tau protein and increase its deposphorylation that may prevent formation of Tau neurofibrilary tangles.
The SensoLyte® Green Pin1 Assay Kit uses fluorogenic substrate that was pretreated to convert into cis isoform. Pin1 changes substrate into trans conformation that is readily cleaved to generate fluorescent signal which can be monitored at Ex/Em=490/520nm. Increase in fluorescence intensity is directly proportional to the Pin1 activity.
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Citations
New PIN1 inhibitors identified through a pharmacophore-driven, hierarchical consensus docking strategy
J Enzyme Inhibit Med Chem . 2021 Dec 11 ; 37(1) 145 | DOI : 10.1080/14756366.2021.1979970
- G. Poli
- et al
Virtual screening identifies a PIN1 inhibitor with possible
J Cell Physiol . 2019 Jan 29 ; | DOI : 10.1002/jcp.28224
- C. Russo Spena
- et al
BCR-ABL enhances the prolyl isomerase activity of Pin 1 by interacting with DAPK1 in ph+ ALL
Cancer Med . 2018 Jun 01 ; 7(6) 2530 | DOI : 10.1002/cam4.1478
- W. Cao
- et al
PIN1 in hepatocellular carcinoma is associated with TP53 gene status
Oncol Rep . 2016 Oct 01 ; 36(4) 2405 | DOI : https://doi.org/10.3892/or.2016.5001
- JS. Bae
- et al
References
Epigallocatechin-gallate Suppresses Tumorigenesis by Directly Targeting Pin1
Cancer Prev Res . 2011 Sep 01 ; 4(9) 1366 | DOI : 10.1158/1940-6207.CAPR-11-0301
- D.V. Urusova
- et al
Pin1 inhibitors: Pitfalls, progress and cellular pharmacology
Biorg Med Chem Lett . 2013 Aug 01 ; 23(15) 4283 | DOI : https://doi.org/10.1016/j.bmcl.2013.05.088
- JD. Moore
- A. Potter