Pure and full length recombinant enzyme
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Hsp10 (human, recombinant)

Item No. 23405

Technical Information
Synonyms
  • CPN10
  • Early-Pregnancy Factor
  • Heat Shock Protein 10
Purity
≥90% estimated by SDS-PAGE
Source
Full length, N-terminally His-tagged human Hsp10 recombinant protein expressed in E. coli
Amino Acids
2-102 (full length)
MW
13.0 kDa
50 mM HEPES, pH 8.0, with 150 mM sodium chloride and 10% glycerol
UniProt Accession №
P61604
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

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    Product Description

    Heat shock protein 10 (Hsp10) has a vital role in cellular function, where it assists in the folding and unfolding of mitochondrial proteins, assembly of multiprotein complexes, and is involved with cellular processes such as apoptosis and carcinogenesis.1,2,3 Together with Hsp60, the Hsp10 protein forms a complex that is the mitochondrial equivalent of the bacterial chaperonin complex GroEL/GroES.4

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Fan, W., Fan, S.-S., Feng, J., et alElevated expression of HSP10 protein inhibits apoptosis and associates with poor prognosis of astrocytoma. PLoS One 12(10), e0185563 (2017).

    2. Samali, A., Cai, J., Zhivotovsky, B., et alPresence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells. EMBO J. 18(8), 2040-2048 (1999).

    3. Capello, F., Di Stefano, A., David, S., et alHsp60 and Hsp10 down-regulation predicts bronchial epithelial carcinogenesis in smokers with chronic obstructive pulmonary disease. Cancer 107(10), 2417-2424 (2006).

    4. Böttinger, L., Oeljeklaus, S., Gulard, B., et alMitochondrial heat shock protein (Hsp) 70 and Hsp10 cooperate in the formation of Hsp60 complexes. The Journal of Biological Chemisty 290(18), 11611-11622 (2015).