Analytical Data
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Gene name
degP
- Application
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Alternative Names
degP；htrA；ptd；Periplasmic serine endoprotease DegP
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Species
E.coli
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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
P0C0V0
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Expression Region
27-474aa
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AA Sequence
AETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ
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Molecular Weight
48.8 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
DegP, a periplasmic protease and chaperone found in Gram-negative bacteria, plays a crucial role in maintaining protein homeostasis under stress conditions. It is involved in the degradation of misfolded proteins and the facilitation of the proper folding of newly synthesized proteins in the periplasm. DegP is typically activated upon the accumulation of unfolded protein substrates, leading to its oligomerization and enhanced proteolytic activity. Researchers have turned their attention to DegP for several reasons, including its potential as a target for antibiotic development, as inhibiting its function may lead to the accumulation of toxic proteins in bacterial pathogens. Furthermore, the study of DegP can provide insights into the broader mechanisms of protein quality control and stress responses in bacteria. Recombinant production of DegP has allowed for detailed investigations into its structure, function, and interaction with substrates, enabling the elucidation of its mechanism of action. Understanding the intricacies of DegP not only contributes to the fundamental knowledge of bacterial physiology but also paves the way for novel therapeutic strategies against multidrug-resistant bacteria, making it a significant focus in microbiological and biochemical research. As scientists continue to explore the various facets of DegP, its role in bacterial survival and pathogenicity remains a vital area of study, showcasing the importance of proteases in the complex landscape of microbial life.
