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Hspe1 recombinant protein :: 10 kDa heat shock protein, mitochondrial (Hspe1) Recombinant Protein

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Catalog # MBS1335133
Unit / Price
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  0.05 mg (E-Coli)  /  $495 +1 FREE 8GB USB
  0.05 mg (Yeast)  /  $645 +1 FREE 8GB USB
  0.2 mg (E-Coli)  /  $660 +1 FREE 8GB USB
  0.5 mg (E-Coli)  /  $725 +1 FREE 8GB USB
  0.2 mg (Yeast)  /  $880 +1 FREE 8GB USB
  0.05 mg (Baculovirus)  /  $885 +1 FREE 8GB USB
  0.5 mg (Yeast)  /  $990 +1 FREE 8GB USB
  1 mg (E-Coli)  /  $1,085 +1 FREE 8GB USB
  0.05 mg (Mammalian-Cell)  /  $1,120 +1 FREE 8GB USB
  0.1 mg (Baculovirus)  /  $1,265 +1 FREE 8GB USB
  1 mg (Yeast)  /  $1,565 +1 FREE 8GB USB
  0.5 mg (Baculovirus)  /  $1,665 +2 FREE 8GB USB
  0.1 mg (Mammalian-Cell)  /  $1,830 +2 FREE 8GB USB
  1 mg (Baculovirus)  /  $2,595 +3 FREE 8GB USB
Hspe1 recombinant protein
Product Name

10 kDa heat shock protein, mitochondrial (Hspe1), Recombinant Protein

Full Product Name

Recombinant Mouse 10 kDa heat shock protein, mitochondrial (Hspe1)

Product Synonym Gene Name
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
2-102aa, Full Length of Mature Protein
Sequence
AGQAFRKFLP LFDRVLVERS AAETVTKGGI MLPEKSQGKV LQATVVAVGS GGKGKSGEIE PVSVKVGDKV LLPEYGGTKV VLDDKDYFLF RDSDILGKYV D
3D Structure
ModBase 3D Structure for Q64433
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Purity/Purification
>85% (SDS-PAGE) (lot specific)
Form/Format
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
Species
Mouse
Storage Buffer
Tris-based buffer, 50% glycerol
Preparation and Storage
Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.
ISO Certification
Manufactured in an ISO 13485:2003 and EN ISO 13485:2012 Certified Laboratory.
Other Notes
Small volumes of Hspe1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
Hspe1 recombinant protein
This gene encodes a major heat shock protein which functions as a chaperonin. Its structure consists of a heptameric ring which binds to another heat shock protein in order to form a symmetric, functional heterodimer which enhances protein folding in an ATP-dependent manner. This gene and its co-chaperonin, HSPD1, are arranged in a head-to-head orientation on chromosome 2.
NCBI/Uniprot data below describe general gene information for Hspe1. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Related Accession #
Molecular Weight
10,963 Da
NCBI Official Full Name
10 kDa heat shock protein, mitochondrial
NCBI Official Synonym Full Names
heat shock protein 1 (chaperonin 10)
NCBI Official Symbol
Hspe1  [Similar Products]
NCBI Official Synonym Symbols
10kDa; Hsp10; mt-cpn10
  [Similar Products]
NCBI Protein Information
10 kDa heat shock protein, mitochondrial
UniProt Protein Name
10 kDa heat shock protein, mitochondrial
UniProt Synonym Protein Names
10 kDa chaperonin; Chaperonin 10; CPN10
UniProt Gene Name
Hspe1  [Similar Products]
UniProt Synonym Gene Names
Hsp10; CPN10  [Similar Products]
UniProt Comments for Hspe1
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.
Research Articles on Hspe1
Precautions
All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
Disclaimer
While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
Products associated with Hspe1 recombinant protein
 Reference Product  PubMed Publications
 Hspd1 recombinant protein  >10 publications with Hspe1 and Hspd1
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