Product Overview
Description
CLPP-00150990 is recombinant human PIN1 protein
Applications
Functional Studies, SDS-PAGE
Protein Length
Full length protein
Nature
Recombinant Protein
Endotoxin Level
< 1.000 Eu/µg
Sequence
MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQGEPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE
Sequence Similarities
Contains 1 PpiC domain. Contains 1 WW domain.
Target Information
Alternative Names
DOD; DODO, Drosophila, homolog of; FLJ40239; FLJ77628; MGC10717; NIMA interacting 1; Peptidyl prolyl cis trans isomerase NIMA interacting 1; Peptidyl prolyl cis/trans isomerase NIMA interacting; Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl-prolyl cis-trans isomerase pin1; Peptidylprolyl cis/trans isomerase NIMA interacting 1; Pin 1; Pin1; PIN1_HUMAN; PPIase Pin1; Prolyl isomerase; Protein (peptidylprolyl cis/trans isomerase) NIMA interacting 1; Protein NIMA interacting 1; Rotamase Pin1; UBL 5; UBL5
Protein 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. 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. 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. 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. 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). Upon IL33-induced lung inflammation, catalyzes cis-trans isomerization of phosphorylated IRAK3/IRAK-M, inducing IRAK3 stabilization, nuclear translocation and expression of pro-inflammatory genes in dendritic cells.
Shipping & Handling
Constituents
0.077% DTT, 0.316% Tris HCl, 20% Glycerol, 0.58% Sodium chloride.
Shipping
Shipped at 4 °C.
Storage
Store at -20 °C or -80 °C.
