• Human PIN1 protein (Recombinant) (No tag) (STJP000789)
  • Human PIN1 protein (Recombinant) (No tag) (STJP000789)
  • Human PIN1 protein (Recombinant) (No tag) (STJP000789)
  • Human PIN1 protein (Recombinant) (No tag) (STJP000789)

Human PIN1 protein (Recombinant) (No tag) (STJP000789)

SKU:
STJP000789

Current Stock:
Host: E. coli
Reactivity: Human
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Recombinant-Human PIN1-No tag protein was developed from e. coli and has a target region of No tag. For use in research applications.
Formulation: Lyophilized from a 0.22 Mu m filtered solution of PBS, pH 7.4. Contact us for customized product form or formulation.
Immunoreactivity: Measured by its binding ability in a functional ELISA. Immobilized Human CTNNB1 Protein at 2 Mu g/mL (100 Mu L/well) can bind PIN1 with a linear range of 7.8-164.3 ng/mL.
Gene Symbol: PIN1
Gene ID: 5300
Uniprot ID: PIN1_HUMAN
Immunogen Region: Met1-Glu163
Immunogen: Recombinant Human PIN1 Protein is produced by E. coli expression system. The target protein is expressed with sequence (Met1-Glu163) of human PIN1 (Accession #NP_006212.1).
Tissue Specificity Expressed in immune cells in the lung (at protein level). The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells.
Post Translational Modifications Phosphorylation at Ser-71 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation. Ser-71 is dephosphorylated upon IL33-stimulation of dendritic cells.
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.
Protein Name Peptidyl-Prolyl Cis-Trans Isomerase Nima-Interacting 1
Peptidyl-Prolyl Cis-Trans Isomerase Pin1
Ppiase Pin1
Rotamase Pin1
Database Links Reactome: R-HSA-1169408
Reactome: R-HSA-5668599
Reactome: R-HSA-6804756
Reactome: R-HSA-6811555
Reactome: R-HSA-936440
Cellular Localisation Nucleus
Nucleus Speckle
Cytoplasm
Colocalizes With Nek6 In The Nucleus
Mainly Localized In The Nucleus But Phosphorylation At Ser-71 By Dapk1 Results In Inhibition Of Its Nuclear Localization
Alternative Protein Names Peptidyl-Prolyl Cis-Trans Isomerase Nima-Interacting 1 protein
Peptidyl-Prolyl Cis-Trans Isomerase Pin1 protein
Ppiase Pin1 protein
Rotamase Pin1 protein
PIN1 protein

Information sourced from Uniprot.org

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