Recombinant Human 10 kDa heat shock protein, mitochondrial(HSPE1)

Code CSB-YP010865HU
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Source Yeast
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Code CSB-EP010865HU
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Source E.coli
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Code CSB-EP010865HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP010865HU
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Source Baculovirus
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Code CSB-MP010865HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names HSPE1
Uniprot No. P61604
Alternative Names 10 kDa chaperonin; 10 kDa heat shock protein mitochondrial; 10 kDa heat shock protein; mitochondrial; CH10_HUMAN; Chaperonin 10; Chaperonin 10 homolog; CPN10; cpn10 homolog; Early pregnancy factor; Early-pregnancy factor; EPF; GROES; GroES homolog; Heat shock 10kD protein 1 chaperonin 10; Heat shock 10kDa protein 1; Heat shock 10kDa protein 1 chaperonin 10; Heat shock protein family E (Hsp10) member; Heat-shock 10-kD protein; Hsp10; Hspe1
Species Homo sapiens (Human)
Expression Region 2-102
Protein Length Full Length of Mature Protein
Tag Info The following tags are available.
N-terminal His-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Background

(From Uniprot)
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
Gene References into Functions
  1. elevated expression of HSP10 protein inhibits apoptosis and associates with poor prognosis of astrocytoma PMID: 29028811
  2. miR-146a, miR-146b, and miR-155 are exerting anti-inflammatory properties by down-regulating IL-6 and IL-8, and influencing the expression of HSP10 in the activated endothelium PMID: 28662100
  3. High expression of HSP10 is negatively associated with estrogen receptor/progesterone receptor status and might be a novel independent biomarker for poor prognosis in invasive ductal breast carcinoma. PMID: 27993580
  4. EPF induces the differentiation of regulatory T cells and increases their immunosuppressive activities. PMID: 27840373
  5. Cpn10 has a role in the spatial regulation of NPAT signaling PMID: 26429916
  6. Hsp10 has a role in nuclear localization and lung cells response to cigarette smoke PMID: 25355063
  7. Data show that that in presence of 300 mg/mL Ficoll the thermodynamic stability of each cpn10 monomer increases by over 30%, whereas the interfaces are stabilized by less than 10%. PMID: 21375247
  8. HSP10 protein was detected only in oocytes from human preantral follicles, whereas in antral follicles, it was localised in oocytes, granulosa cells, theca cells and stroma cells. PMID: 19903031
  9. Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. PMID: 11898127
  10. The low stability of the monomeric unit suggests that folding and assembly reactions for cpn10 are coupled. PMID: 12220543
  11. Cpn10 and placental lactogen are capable of stimulating the synthesis of type I collagen by human osteoblasts in culture PMID: 12703979
  12. Identification of amino acids important for the assembly of the cpn10 heptamer. PMID: 14525625
  13. complex mechanisms are involved in the protection by hsp10 against simulated ischemia and reoxygenation-induced myocyte death PMID: 15059967
  14. The HSP10 plays a role in bone marrow cell differentiation other than being a mitochondrial co-chaperonin. PMID: 15590416
  15. Chaperonin 10 and calgranulin A are identified as markers for diagnosis and screening of endometrial carcinoma. PMID: 15816004
  16. the cpn10 interfaces can adapt to structural alterations without loss of either subunit-subunit affinity or heptamer specificity PMID: 15978542
  17. biophysical analysis of dissociation equilibrium for the heptameric co-chaperonin proteins 10 from Aquifex aeolicus and human mitochondria PMID: 16100270
  18. proteomic analysis of possible role of heat shock protein 10 in colorectal cancer PMID: 16502466
  19. Results describe the time-resolved folding and assembly mechanism of the heptameric co-chaperonin protein 10 (cpn10) in vitro. PMID: 16979655
  20. Investigation of single-nucleotide variations in the Hsp10 gene and their disease-causing potential. PMID: 17072495
  21. In this review, we revise the involvement of Hsp10 in signal transduction pathways and its possible role in cancer etiology. PMID: 17278877
  22. Data show that Hhsp10 formed fibrils from only the acidic unfolded state and Core peptide regions of these protein fibrils were determined by proteolysis followed by a combination of Edman degradation and mass spectroscopy analyses. PMID: 18329043
  23. The effects of cpn 10 on cells of the oligodendrocyte lineage, were assessed. PMID: 18465204
  24. In patients with serous ovarian carcinomas, gene expression analysis coupled with immunohistochemistry allowed the identification of HSP10 as an independent factor of progression-free survival. PMID: 18500265
  25. Results describe a novel function of chaperonin 10 as a general differentiation factor, not limited to erythroid cells, and show how this biological effect is mediated by GSK-3alpha/beta. PMID: 19142874
  26. HSP10 was identified as a new autoantigen in both autoimmune pancreatitis and fulminant type 1 diabetes. PMID: 19520060

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Subcellular Location Mitochondrion matrix
Protein Families GroES chaperonin family
Database Links

HGNC: 5269

OMIM: 600141

KEGG: hsa:3336

STRING: 9606.ENSP00000233893

UniGene: Hs.1197


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