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Pin1 (NM_023371) Mouse Tagged ORF Clone Lentiviral Particle
CAT＃: MR201342L4V
- LentiORF®
-
Lenti ORF particles, Pin1 (GFP-tagged) - Mouse protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1 (Pin1), 200ul, >10^7 TU/mL
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CNY 8,360.00
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Specifications
| Product Data | |
| Product Name | Pin1 (NM_023371) Mouse Tagged ORF Clone Lentiviral Particle |
| Synonyms | 0610025L01Rik; D9Bwg1161e |
| Vector | pLenti-C-mGFP-P2A-Puro |
| ACCN | NM_023371 |
| ORF Size | 498 bp |
| Sequence Data |
The ORF insert of this clone is exactly the same as(MR201342).
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| OTI Disclaimer | The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info |
| OTI Annotation | This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene. |
| Reference Data | |
| RefSeq | NM_023371.2 |
| RefSeq Size | 3808 bp |
| RefSeq ORF | 498 bp |
| Locus ID | 23988 |
| Gene Summary | 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 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. 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 (By similarity). 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 (By similarity). 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) (By similarity).[UniProtKB/Swiss-Prot Function] |
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