Peptidyl-Prolyl Cis-Trans Isomerase NIMA-Interacting 1 (PIN1) Peptide
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Description
Peptidyl-Prolyl Cis-Trans Isomerase NIMA-Interacting 1 (PIN1) Peptide is a synthetic peptide.
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Peptidyl-Prolyl Cis-Trans Isomerase NIMA-Interacting 1 (PIN1) |
| Host | Synthetic |
| Recommended Dilution | BL (predicted): 0.5 mg/ml. Optimal dilutions/concentrations should be determined by the end user. |
| Conjugation | Unconjugated |
| Observed MW | Sequence Fragment: Internal region: C-KHSQSRRPSSWRQEKITR |
| Size 1 | 100 µg |
| Form | Lyophilized Reconstitute in deionized water. |
| Tested Applications | P-ELISA |
| Buffer | Prior to lyophilization: Deionized water. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| Gene ID | 5300, 23988, 298696 |
| NCBI Accession | NP_006212.1 |
| Background | Protein PIN1 |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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Human PIN1 (Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1) ELISA Kit
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PIN1 antibody
Peptidyl-prolyl cis/trans isomerase(PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro(pSer/Thr-Pro) motifs in a subset of proteins, resulting in conformational changes in the proteins(PubMed:21497122, PubMed:22033920). Displays a preference for an acidic residue N-terminal to the isomerized proline bond. 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).
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