Analytical Data
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Gene name
CLPP
- Application
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Alternative Names
CLPP;ATP-dependent Clp protease proteolytic subunit. mitochondrial
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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
Q16740
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Expression Region
1-277aa
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AA Sequence
MWPGILVGGARVASCRYPALGPRLAAHFPAQRPPQRTLQNGLALQRCLHATATRALPLIPIVVEQTGRGERAYDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKKPIHMYINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAASMGSLLLAAGTPGMRHSLPNSRIMIHQPSGGARGQATDIAIQAEEIMKLKKQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDKVLVHPPQDGEDEPTLVQKEPVEAAPAAEPVPAST
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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
Related Products
Protein Description
CLPP (caseinolytic peptidase B) is a crucial proteolytic enzyme belonging to the Clp protease family, primarily involved in protein quality control and degradation within various cellular environments. The significance of CLPP has garnered attention due to its role in maintaining cellular homeostasis, particularly under stress conditions that can lead to protein aggregation and dysfunction. Research on CLPP has expanded significantly, as it is implicated in various biological processes, including protein maturation, turnover, and the regulation of metabolic pathways, making it a potential target for therapeutic interventions. Furthermore, abnormalities in CLPP function are associated with several diseases, including neurodegenerative disorders and cancer, underscoring the importance of understanding its structural and functional characteristics. Recombination techniques have allowed for the production of CLPP recombinant proteins, facilitating detailed studies on their enzymatic activity, substrate specificity, and interactions with other cellular components. This research not only advances our fundamental understanding of proteolytic systems but also opens avenues for developing novel strategies to manipulate CLPP activity, potentially leading to innovative therapies for diseases linked to proteostasis imbalance. Thus, examining CLPP's functionality through recombinant protein studies is critical for uncovering its therapeutic potential and biological significance.











