Anti-Pin1 Antibody Picoband® Fluoro647 Conjugated

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, also called DOD, is an enzyme that in humans is encoded by the PIN1 gene. It is mapped to 19p13.2. The enzyme binds to a subset of proteins and thus plays a role as a post phospho PIN1rol in regulating protein function. Studies have shown that the deregulation of PIN1 may play a pivotal role in various diseases. Notably, the up-regulation of PIN1 may be implicated in certain cancers, and the down-regulation of Pin1 may be implicated in Alzheimer's disease. Inhibitors of PIN1 may have therapeutic implications for cancer and immune disorders. PIN1 activity regulates the outcome of proline-ed kinase (e.g. MAPK, CDK or GSK3) signalling and consequently regulates cell proliferation (in part through control of cyclin D1 levels and stability) and cell survival. PIN1 also has an essential role in maintaining cell proliferation and regulating cyclin D1 function.

Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr- Pro) motifs in a subset of proteins, resulting in conformational changes in the proteins (PubMed:21497122, PubMed:22033920) . Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK (PubMed:16644721) . Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation (PubMed:15664191) . Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner (PubMed:17828269) . Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN (PubMed:22608923) . .

1. Liou, Y.-C., Ryo, A., Huang, H.-K., Lu, P.-J., Bronson, R., Fujimori, F., Uchida, T., Hunter, T., Lu, K. P. Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes. Proc. Nat. Acad. Sci. 99: 1335-1340, 2002. 2. Lu, KP; Finn G; Lee TH; Nicholson LK (Oct 2007) . Prolyl cis-trans isomerization as a molecular timer.Nat. Chem. Biol. (United States) 3 (10) : 619–29.

Nucleus . Nucleus speckle . Cytoplasm . Colocalizes with NEK6 in the nucleus (PubMed:16476580) . Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization (PubMed:21497122) . .