Analytical Data
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Gene name
ClpC1 NTD
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简介
ClpC1 NTD Protein, the ATP-dependent specificity component of the Clp protease, directs the protease to specific substrates and exhibits chaperone functions independently of ClpP. It plays a crucial role in the targeted degradation of substrates, such as the anti-sigma-E factor RseA, in the presence of ClpP2. ClpC1 NTD Protein, Mycobacterium tuberculosis is the recombinant ClpC1 NTD protein, expressed by E. coli , with tag free.
- Application
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Alternative Names
clpC1; ATP-dependent Clp protease ATP-binding subunit ClpC1
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Species
Others
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P9WPC9
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Expression Region
M1-Y145
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Protein Length
Partial
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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
ClpC1, a member of the ATP-dependent Clp protease family, plays a crucial role in protein quality control and the degradation of misfolded proteins in bacterial cells. The N-terminal domain (NTD) of ClpC1 is particularly interesting due to its involvement in substrate recognition and the regulation of proteolytic activity. Recent studies have highlighted the importance of ClpC1 NTD in various physiological processes, including stress responses and cell division, suggesting that it may be a potential target for antibiotic development. Additionally, understanding the structural and functional properties of ClpC1 NTD could provide insights into its mechanism of action and its interactions with other cellular components. Researchers have focused on the recombinant production of ClpC1 NTD to facilitate biochemical characterization and to explore its potential as a therapeutic target. By elucidating the structure-function relationships of this domain, scientists aim to identify novel strategies for combating bacterial infections by disrupting the protein homeostasis mechanisms in pathogens. This research underscores the relevance of ClpC1 NTD in microbial physiology and its prospective applications in drug design and development.
