Hspe1 (NM_008303) Mouse Tagged ORF Clone Lentiviral Particle

CAT#: MR200324L4V

  • LentiORF®

Lenti ORF particles, Hspe1 (GFP-tagged) - Mouse heat shock protein 1 (chaperonin 10) (Hspe1), nuclear gene encoding mitochondrial protein, 200ul, >10^7 TU/mL

ORF Plasmid: DDK tGFP



Need custom lentivirus service?
Get a free quote

CNY 8,360.00


货期*
详询

规格
    • 200 ul

Product images

经常一起买 (2)
Lenti ORF control particles of pLenti-C-mGFP-P2A-Puro, >1x10^7 TU/ml, 0.5 ml
    • 500 ul

CNY 2,950.00


One-Wash Lentivirus Titer Kit, HIV-1 p24 ELISA
    • 96 reactions

CNY 5,230.00

Specifications

Product Data
Product Name Hspe1 (NM_008303) Mouse Tagged ORF Clone Lentiviral Particle
Synonyms 10kDa; Hsp10; mt-cpn10
Vector pLenti-C-mGFP-P2A-Puro
ACCN NM_008303
ORF Size 309 bp
Sequence Data
The ORF insert of this clone is exactly the same as(MR200324).
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_008303.3
RefSeq Size 788 bp
RefSeq ORF 309 bp
Locus ID 15528
Gene Summary Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein.[UniProtKB/Swiss-Prot Function]
*Delivery time may vary from web posted schedule. Occasional delays may occur due to unforeseen complexities in the preparation of your product. International customers may expect an additional 1-2 weeks in shipping.
Customer Reviews 
Loading...