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Hsp90aa1 (BC046614) Mouse Tagged ORF Clone Lentiviral Particle
CAT＃: MR210352L4V
- LentiORF®
-
Lenti ORF particles, Hsp90aa1 (GFP-tagged) - Mouse heat shock protein 90kDa alpha (cytosolic), class A member 1 (cDNA clone MGC:54660 IMAGE:6491307), 200ul, >10^7 TU/mL
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CNY 13,205.00
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Specifications
| Product Data | |
| Product Name | Hsp90aa1 (BC046614) Mouse Tagged ORF Clone Lentiviral Particle |
| Synonyms | 86kDa, 89kDa |
| Vector | pLenti-C-mGFP-P2A-Puro |
| ACCN | BC046614 |
| ORF Size | 2199 bp |
| Sequence Data |
The ORF insert of this clone is exactly the same as(MR210352).
|
| 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 | BC046614.1 |
| RefSeq Size | 2800 bp |
| RefSeq ORF | 2201 bp |
| Locus ID | 15519 |
| Gene Summary | Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation.[UniProtKB/Swiss-Prot Function] |
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