Hspe1 (NM_008303) Mouse Recombinant Protein

CAT#: TP500324

Purified recombinant protein of Mouse heat shock protein 1 (chaperonin 10) (Hspe1), with C-terminal MYC/DDK tag, expressed in HEK293T cells, 20ug

Specifications

Product Data

• Species: Mouse
• Expression Host: HEK293T
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  >MR200324 protein sequence
  Red=Cloning site Green=Tags(s)
  
  MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGGKGKSGEIEPVSVKVGDK
  VLLPEYGGTKVVLDDKDYFLFRDSDILGKYVD
  
  TRTRPLEQKLISEEDLAANDILDYKDDDDKV
• Tag: C-MYC/DDK
• Predicted MW: 11 kDa
• Concentration: >0.05 µg/µL as determined by microplate BCA method
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Buffer: 25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol
• Note: For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process.
• Storage: Store at -80°C after receiving vials.
• Stability: Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.

Reference Data

• RefSeq: NP_032329
• Locus ID: 15528
• UniProt ID: Q64433, Q4KL76
• Cytogenetics: 1 C1.2
• Refseq Size: 788
• Refseq ORF: 309
• Synonyms: 10kDa; Hsp10; mt-cpn10
• 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]