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Anti-Pin1 Picoband Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB |
|---|---|
| Primary Accession | Q13526 |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Clonality | Polyclonal |
| Format | Lyophilized |
| Description | Rabbit IgG polyclonal antibody for Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1(PIN1) detection. Tested with WB in Human;Mouse;Rat. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 5300 |
|---|---|
| Other Names | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, 5.2.1.8, Peptidyl-prolyl cis-trans isomerase Pin1, PPIase Pin1, Rotamase Pin1, PIN1 |
| Calculated MW | 18243 MW KDa |
| Application Details | Western blot, 0.1-0.5 µg/ml, Human, Mouse, Rat |
| Subcellular Localization | Nucleus . Nucleus speckle . Cytoplasm . Colocalizes with NEK6 in the nucleus (PubMed:16476580). Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization (PubMed:21497122). . |
| Tissue Specificity | The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells. . |
| Protein Name | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 |
| Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. |
| Immunogen | E.coli-derived human Pin1 recombinant protein (Position: M1-E163). Human Pin1 shares 95% amino acid (aa) sequence identity with mouse Pin1. |
| Purification | Immunogen affinity purified. |
| Cross Reactivity | No cross reactivity with other proteins |
| Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
| Sequence Similarities | Contains 1 PpiC domain. |
| Name | PIN1 |
|---|---|
| Function | Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs (PubMed:21497122, PubMed:23623683, PubMed:29686383). By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes (PubMed:21497122, PubMed:22033920, PubMed:23623683). 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). 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 (PubMed:29686383). |
| Cellular Location | Nucleus. Nucleus speckle. Cytoplasm Note=Colocalizes with NEK6 in the nucleus (PubMed:16476580). Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization (PubMed:21497122) |
| Tissue Location | Expressed in immune cells in the lung (at protein level) (PubMed:29686383). The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells |
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Provided below are standard protocols that you may find useful for product applications.
Background
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, also called DOD, is an enzyme that in humans is encoded by the PIN1 gene. It is mapped to 19p13.2. The enzyme binds to a subset of proteins and thus plays a role as a post phospho PIN1rol in regulating protein function. Studies have shown that the deregulation of PIN1 may play a pivotal role in various diseases. Notably, the up-regulation of PIN1 may be implicated in certain cancers, and the down-regulation of Pin1 may be implicated in Alzheimer's disease. Inhibitors of PIN1 may have therapeutic implications for cancer and immune disorders. PIN1 activity regulates the outcome of proline-directed kinase (e.g. MAPK, CDK or GSK3) signalling and consequently regulates cell proliferation (in part through control of cyclin D1 levels and stability) and cell survival. PIN1 also has an essential role in maintaining cell proliferation and regulating cyclin D1 function.
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