|Application ||WB, IHC-P, E, IP|
|Reactivity||Human, Monkey, Bovine, Dog|
|Dilution||ELISA (1:2500-1:10000), IHC-P (5 µg/ml), IP (1:100), WB (1:500-1:3000) ,|
|Other Names||Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, 126.96.36.199, Peptidyl-prolyl cis-trans isomerase Pin1, PPIase Pin1, Rotamase Pin1, PIN1|
|Target/Specificity||Human Pin1. A BLAST analysis was used to suggest cross-reactivity with Pin1 from human, dog, bovine and monkey based on a 100% homology with the immunizing sequence. Expect partial reactivity with Pin1 from mouse and rat sources based on 92% sequence ...|
|Reconstitution & Storage||Long term: -20°C; Short term: -20°C|
|Precautions||PIN1 Antibody (Internal) 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. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes (PubMed:21497122, PubMed:22033920, Ref. 21). Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. 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). May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR) (PubMed:23623683, PubMed:27561354).|
|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|
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Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. 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. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner.
Lu K.P.,et al.Nature 380:544-547(1996).
Ebert L.,et al.Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
Kalnine N.,et al.Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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