PIN1 Protein, Human

The PIN1 protein is a peptidyl-prolyl cis/trans isomerase that complexly regulates multiple cellular processes by binding and isomerizing phosphorylated Ser/Thr-Pro motifs. This molecular switch induces conformational changes in phosphorylated proteins that affect mitosis, kinase activity, oncogene transactivation, centrosome amplification, and cell transformation. PIN1 Protein, Human is the recombinant human-derived PIN1 protein, expressed by E. coli , with tag free. The total length of PIN1 Protein, Human is 163 a.a., with molecular weight of ~18 kDa.

PIN1 Protein, a peptidyl-prolyl cis/trans isomerase (PPIase), intricately participates in multiple cellular processes by binding to and isomerizing specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. This molecular switch induces conformational changes in phosphorylated proteins, influencing diverse cellular pathways. With a preference for acidic residues N-terminally to the proline bond, PIN1 regulates mitosis by interacting with NIMA, attenuating its mitosis-promoting activity, and down-regulating the kinase activity of BTK. It transactivates oncogenes, induces centrosome amplification, chromosome instability, and cell transformation. Moreover, PIN1 is crucial for the dephosphorylation and recycling of RAF1, binding and targeting PML and BCL6 for degradation, and acting as a regulator of the JNK cascade by disrupting FBXW7 dimerization. PIN1's involvement extends to DNA repair processes, where it influences the balance between error-prone non-homologous end joining (NHEJ) and error-free homologous recombination (HR). During IL33-induced lung inflammation, PIN1 catalyzes cis-trans isomerization of phosphorylated IRAK3/IRAK-M, contributing to IRAK3 stabilization, nuclear translocation, and the expression of pro-inflammatory genes in dendritic cells.

Human

E. coli

Tag Free

Q13526 (M1-E163)

5300  [NCBI]

Approximately 18 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.