|Calculated MW||18.2 kDa (163 aa)|
|Other Names||Protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1, NIMA-interacting protein 1, DOD, UBL5, Rotamase Pin1, PPIase Pin1.|
|Sequence||MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGGKNGQG EPARVRCSHL LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RTE|
|Storage||-80°C; 1 mg/ml solution in 20 mM Tris-HCl buffer (pH 7.5) containing 100 mM NaCl, 5 mM DTT, 20% glycerol.|
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Provided below are standard protocols that you may find useful for product applications.
Human Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA ,PLK I, Wee, and Myt1 kinases), several transcription factors like β-Catenin, c-Jun, and the tumor suppressor protein p53 , and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1.
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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