Recombinant Escherichia coli Periplasmic serine endoprotease DegP (degP)

Code CSB-EP314631ENV
MSDS
Size US$388
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
degP
Uniprot No.
Research Area
Others
Alternative Names
degP; htrA; ptd; b0161; JW0157; Periplasmic serine endoprotease DegP; EC 3.4.21.107; Heat shock protein DegP; Protease Do
Species
Escherichia coli (strain K12)
Source
E.coli
Expression Region
27-474aa
Target Protein Sequence
AETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
62.8kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-SUMO-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

The production of this recombinant E.coli degP protein is just like all recombinant proteins. The process involved transfecting E.coli cells with DNA vector containing the template of recombinant DNA. The E.coli cells containing the template were then cultured so that they could transcribe and translate the degP protein. N-terminal 6xHis-SUMO tag was used in the process. The purity is 90% determined by SDS-PAGE.

degP is a gene providing instructions for making a protein called periplasmic serine endoprotease DegP (also known as heat shock protein DegP or protease Do). DegP protein belongs to the peptidase S1C family. DegP is a heat shock protein induced in response to pac overexpression, suggesting that the protein could possibly suppress the physiological toxicity caused by pac overexpression. Increasing evidence indicates that the production of soluble recombinant penicillin acylase in Escherichia coli can be enhanced via coexpression of a periplasmic protease/chaperone, DegP.

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Target Background

Function
DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolytic activity is essential for the survival of cells at elevated temperatures. It can degrade IciA, Ada, casein, globin and PapA. DegP shares specificity with DegQ. DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP).
Gene References into Functions
  1. Our results suggest that YjfN is a novel "suicide activator" for DegP that enhances DegP proteolysis under misfolded protein stress. PMID: 28947671
  2. Investigated the influence of amino acid substitutions located within the LD loop on the kinetics of a model substrate cleavage as well as on the dynamics of the oligomeric structure of HtrA. We found that the mutations that were expected to disturb the loop's structure and/or interactions with the remaining regulatory loops severely diminished the proteolytic activity of HtrA. PMID: 27469236
  3. In the present review, we summarize recent advances in the characterization of these key factors, with a special emphasis on the multifunctional protein DegP. PMID: 25849907
  4. The lack of the disulfide within LA affected the stability and the overall structure of the HtrA molecule. PMID: 25710793
  5. Sensitive activation and cage assembly needs covalent linkage of distinct substrate sequences that affect degradation (degrons); 1 degron binds the DegP active site, a 2nd degron binds a separate tethering site in PDZ1 of a substrate-bound DegP dodecamer. PMID: 21458668
  6. Formation of contacts between the apical parts (residues 231-234) of the L2 loops within the HtrA trimer, in particular the residue D232, was shown to play a crucial role in the activation process of HtrA. PMID: 20515644
  7. Effector-peptide binding to the PDZ domain of DegP induces oligomer conversion from resting hexameric DegP6 into proteolytically active 12-mers and 24-mers. PMID: 20581825
  8. The combined introduction of loop L2 and PDZ domain 1 of DegP into DegS converted DegS even further into a DegP-like protease. PMID: 20184896
  9. the osmoregulation of the expression of htrA gene; role of the nucleoid associated proteins H-NS and Hha in the repression of htrA expression at low osmolarity PMID: 16143461
  10. the N-terminal alpha-helix is an important functional domain for inhibition of the Cpx pathway and that CpxP is subject to DegP-dependent proteolysis PMID: 16166523
  11. CpxP functions as a periplasmic adaptor protein that is required for the effective proteolysis of a subset of misfolded substrates by the DegP protease PMID: 16303867
  12. Results show that the functional unit for the protease and chaperone activities of DegP is a trimer and that neither a cavity of specific dimensions nor the presence of an enclosed cavity appears to be essential for its protease and chaperone activities. PMID: 17122339
  13. HtrA may protect the bacterial cells from deleterious effects of heat shock not only by degrading the damaged proteins but by combination of the proteolytic and chaperoning activities PMID: 17485069
  14. This article summarizes recent studies regarding the HtrA family of proteins, their structure, regulation and function. It also presents practical applications of this knowledge and perspective of its use in the future. PMID: 17718385
  15. HtrA can in fact act as a protease at low temperatures. PMID: 19047732
  16. Review show that DegP adopts various forms, depending on the surrounding environment and the availability of a substrate. PMID: 19465652

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Subcellular Location
Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.
Protein Families
Peptidase S1C family
Database Links
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