Analytical Data
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Gene name
clpC
- Application
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Alternative Names
clpC；HSP93-III；Chaperone Protein ClpC2. chloroplastic
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99W78
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Expression Region
1-147aa
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AA Sequence
MLFGRLTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVIEEVEKLIGHGQDHVGTLHYTPRAKKVIELSMDEARKLHHNFVGTEHILLGLIRENEGVAARVFANLDLNITKARAQVVKALGNPEM
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Molecular Weight
32.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
ClpC is a crucial ATP-dependent protease belonging to the Clp (Caseinolytic protease) family, implicated in protein quality control and cellular responses to stress in various organisms, including bacteria and eukaryotes. The study of ClpC recombinant proteins has gained significant attention due to their essential roles in protein degradation, translocation, and unfolding, which are vital for maintaining cellular homeostasis and regulating physiological processes. Understanding the function and regulation of ClpC can provide insights into fundamental biological mechanisms, as well as potential targets for novel antimicrobial therapies. Research has shown that ClpC interacts with specific adaptor proteins, influencing substrate recognition and processing. Furthermore, dysregulation of ClpC has been linked to various diseases, highlighting the importance of this protease in both health and disease. The recombinant expression of ClpC facilitates biochemical characterization and functional assays, advancing our knowledge of its structure and mechanism of action. By elucidating these aspects, scientists hope to uncover the therapeutic potential of targeting ClpC in diseases related to protein misfolding and degradation. Overall, the exploration of ClpC recombinant proteins not only enriches our understanding of proteostasis but also underscores its relevance in the development of intervention strategies against pathologies associated with proteolytic dysfunction.
