|Application ||WB, E|
|Other Accession||NP_006212, 5300, 23988 (mouse), 298696 (rat)|
|Predicted||Human, Mouse, Dog|
|Calculated MW||18243 Da|
|Other Names||Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, 18.104.22.168, Peptidyl-prolyl cis-trans isomerase Pin1, PPIase Pin1, Rotamase Pin1, PIN1|
|Format||0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Goat Anti-PIN1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|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).|
|Cellular Location||Nucleus. Nucleus speckle. Cytoplasm. Note=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)|
|Tissue Location||The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Peptidyl-prolyl cis/trans isomerases (PPIases; EC 22.214.171.124), such as PIN1, catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds. PIN1 is the only PPIase that specifically binds to phosphorylated ser/thr-pro motifs to catalytically regulate the post-phosphorylation conformation of its substrates. PIN1-catalyzed conformational regulation has a profound impact on key proteins involved in the regulation of cell growth, genotoxic and other stress responses, the immune response, germ cell development, neuronal differentiation, and survival (review by Lu and Zhou, 2007 [PubMed 17878917]).
A PIN1 polymorphism that prevents its suppression by AP4 associates with delayed onset of Alzheimer's disease. Ma SL, et al. Neurobiol Aging, 2010 Jun 24. PMID 20580132.
Uncoating of human immunodeficiency virus type 1 requires prolyl isomerase Pin1. Misumi S, et al. J Biol Chem, 2010 Aug 13. PMID 20529865.
The prolyl isomerase Pin1 induces LC-3 expression and mediates tamoxifen resistance in breast cancer. Namgoong GM, et al. J Biol Chem, 2010 Jul 30. PMID 20479004.
Elevated PIN1 expression by C/EBPalpha-p30 blocks C/EBPalpha-induced granulocytic differentiation through c-Jun in AML. Pulikkan JA, et al. Leukemia, 2010 May. PMID 20376080.
Membrane permeable cyclic peptidyl inhibitors against human Peptidylprolyl Isomerase Pin1. Liu T, et al. J Med Chem, 2010 Mar 25. PMID 20180533.
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