Hspd1 (NM_010477) Mouse Tagged ORF Clone Lentiviral Particle

CAT#: MR222671L4V

Lenti ORF particles, Hspd1 (GFP-tagged) - Mouse heat shock protein 1 (chaperonin) (Hspd1), nuclear gene encoding mitochondrial protein, 200ul, >10^7 TU/mL

Specifications

Product Data

• Type: Mouse Tagged ORF Clone
• Tag: mGFP
• Symbol: Hspd1
• Synonyms: 60kDa; CPN60; HSP-60; HSP-65; Hsp60
• Mammalian Cell Selection: Puromycin
• Vector: pLenti-C-mGFP-P2A-Puro
• ACCN: NM_010477
• ORF Size: 1719 bp
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(MR222671).
• 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_010477.4, NP_034607.3
• RefSeq Size: 2347 bp
• RefSeq ORF: 1722 bp
• Locus ID: 15510
• UniProt ID: P63038
• Cytogenetics: 1 C1.2
• Gene Summary: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, 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]