Analytical Data
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Gene name
DEGP12
- Application
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Alternative Names
DEGP12; At3g16550; MDC8.18Putative protease Do-like 12; mitochondrial; EC 3.4.21.-
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Species
Arabidopsis thaliana
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9LK70
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Expression Region
25-499aa
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Molecular Weight
69.5 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
DEGP12 is a recombinant protein that has garnered significant interest in the field of biochemistry and molecular biology due to its potential roles in cellular processes and enzyme regulation. Originally identified in certain microorganisms, DEGP12 is part of the DegP (Deglycase and Protease) family of proteins, which are known to possess chaperone-like functions and proteolytic activity. The study of DEGP12 is crucial for understanding its structure-function relationships, mechanisms of action, and potential applications in biotechnology and medicine. Research has demonstrated that DEGP12 may play a vital role in protein quality control, aiding in the refolding of misfolded proteins and facilitating their degradation. This makes it an essential component in the maintenance of cellular homeostasis, particularly under stress conditions. Additionally, the recombinant expression of DEGP12 allows for the exploration of its interactions with substrates and inhibitors, which can uncover insights into its regulatory mechanisms. The investigation of DEGP12 not only advances our knowledge of protein biochemistry but also opens avenues for developing therapeutic strategies targeting proteostasis-related diseases. As such, DEGP12 serves as a valuable model for studying the intricate balance of protein synthesis, folding, and degradation in living organisms.
