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Recombinant Human HSP10/EPF Protein, CF 50 UG

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產(chǎn)品介紹

    基本參數(shù)

    詳細(xì)說明

    • Purity

      >85%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie? Blue stain

    • Activity

      HSP10/HSPE1 is a molecular chaperone that assists in the folding of nascent polypeptides and the refolding of denatured proteins.  Reaction conditions will need to be optimized for each specific application.  IMPORTANT: HSP10/HSPE1 works in conjunction with HSP60/HSPD1 (Catalog # AP-140) and both proteins are required for enzymatic activity.   For in vitro use we recommend an initial HSP60/HSPD1 concentration of 2-3 μM, and HSP10/HSPE1 concentration equimolar (or above) to HSP60/HSPD1.

    • Source

      E. coli-derived Accession # P61604

    • Accession #

    • Predicted Molecular Mass

      11 kDa

    AP-150

     

    Formulation      

    X mg/ml (X μM) in 50 mM HEPES pH 7.5, 100 mM NaCl, 1 mM TCEP





    Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.


    Stability & Storage:       Use a manual defrost freezer and avoid repeated freeze-thaw cycles.      

    • 12 months from date of receipt, -70 °C as supplied.

    • 3 months, -70 °C under sterile conditions after opening.


    Background: HSP10/EPF

    HSP10 (also known as Chaperonin 10) is the eukaryotic homologue of the prokaryotic GroES chaperones. This protein is found mainly in mitochondria, but can also be detected in cytosol and extracellular fluids including peripheral blood. Together with HSP60 (also known as Chaperonin 60), HSP10 plays an essential role in the translocation and refolding of proteins from the cytosol into the mitochondrial matrix. Under physiological conditions, HSP60 creates two stacked heptameric rings that form a pair of central hydrophobic cavities. After an unfolded substrate protein enters one of the cavities it is capped by a heptameric HSP10 complex, thereby trapping the unfolded protein. Structural rearrangement of the substrate-containing cavity is effected via HSP60-mediated ATP hydrolysis; this changes the lining of the cavity from hydrophobic to hydrophilic and helps promote refolding of the substrate protein. Binding of ATP to HSP60 subunits on the distal ring of the complex then causes the dissociation of the HSP10 cap complex and concomitant release of the substrate protein from the proximal cavity. If the protein is not completely folded, it can be further processed by the HSP60/HSP10 complex, or can interact with other chaperoning systems.

    • References:

      1. Cappello F, et al. (2008) Cancer Biol. Therapy 7: 801-809

      2. Hartl F.U. & Hayer-Hartl M. (2009) Nat. Struc. Mol. Biol. 16: 574-581

    • Long Name:

      Heat Shock 10 kDa Protein 1

    • Entrez Gene IDs:

      3336 (Human); 69253 (Mouse)

    • Alternate Names:

      10 kDa chaperonin; 10 kDa heat shock protein, mitochondrial; Chaperonin 10 Homolog; Chaperonin 10; CPN10HSP10; Early-pregnancy factor; EPF; GroES; heat shock 10kD protein 1 (chaperonin 10); heat shock 10kDa protein 1 (chaperonin 10); HSP10; HSPE1



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