Anti-Pin1 Antibody

Boster Bio Anti-Pin1 Antibody catalog # A00467-1. Tested in ELISA, IF, IHC applications. This antibody reacts with Human, Mouse, Rat.

Product Specifications

Synonyms

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1;5.2.1.8; Peptidyl-prolyl cis-trans isomerase Pin1; PPIase Pin1; Rotamase Pin1; PIN1;

Gene Name

PIN1

UniProt

Q13526

Host

Rabbit

Reactivity

Human, Mouse, Rat

Immunogen

The antiserum was produced against synthesized peptide derived from human Pin1. AA range:1-50

Clonality

Polyclonal

Tissue Specificity

The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells.

Applications

IHC, IF, ELISA

Purification

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

Concentration

1 mg/ml

Form

Liquid

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) .