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Periplasmic Serine Endoprotease Degp (degP) Escherichia Coli Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS1198532

DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions.… More details

$445 / 0.02 mg (Yeast) +1 FREE 8GB USB
Product Documentation
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Sample Manual Insert View PDF
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Testing Data View PDF
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Material Safety Data Sheet View PDF
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Technical Datasheet View PDF
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Product Overview

Online Datasheet in PDF
Product Name
Periplasmic serine endoprotease DegP, Recombinant Protein
Full Product Name
Recombinant Escherichia coli Periplasmic serine endoprotease DegP
Product Gene Name
Product Synonym Names
Heat shock protein DegP; Protease Do
Sequence
AETSSATTAQ QMPSLAPMLE KVMPSVVSIN VEGSTTVNTP RMPRNFQQFF GDDSPFCQEG SPFQSSPFCQ GGQGGNGGGQ QQKFMALGSG VIIDADKGYV VTNNHVVDNA TVIKVQLSDG RKFDAKMVGK DPRSDIALIQ IQNPKNLTAI KMADSDALRV GDYTVAIGNP FGLGETVTSG IVSALGRSGL NAENYENFIQ TDAAINRGNS GGALVNLNGE LIGINTAILA PDGGNIGIGF AIPSNMVKNL TSQMVEYGQV KRGELGIMGT ELNSELAKAM KVDAQRGAFV SQVLPNSSAA KAGIKAGDVI TSLNGKPISS FAALRAQVGT MPVGSKLTLG LLRDGKQVNV NLELQQSSQN QVDSSSIFNG IEGAEMSNKG KDQGVVVNNV KTGTPAAQIG LKKGDVIIGA NQQAVKNIAE LRKVLDSKPS VLALNIQRGD STIYLLMQ
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
48.8 kDa
Sequence Positions
27-474aa, Full Length of Mature Protein
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
3D Structure
ModBase 3D Structure for P0C0V0
ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for degP recombinant protein

Sequence analysis and regulation of the htrA gene of Escherichia coli a sigma 32-independent mechanism of heat-inducible transcription.Lipinska B., Sharma S., Georgopoulos C.Nucleic Acids Res. 16:10053-10067(1988) Systematic sequencing of the Escherichia coli genome analysis of the 2.4-4.1 min (110,917-193,643 bp) region.Fujita N., Mori H., Yura T., Ishihama A.Nucleic Acids Res. 22:1637-1639(1994) Sequence of minutes 4-25 of Escherichia coli.Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. The complete genome sequence of Escherichia coli K-12.Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.Science 277:1453-1462(1997) Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.Mol. Syst. Biol. 2:E1-E5(2006) Primary structure of the deoxyguanosine triphosphate triphosphohydrolase-encoding gene (dgt) of Escherichia coli.Quirk S., Bhatnagar S.K., Bessman M.J.Gene 89:13-18(1990) Structure and regulation of the gene for dGTP triphosphohydrolase from Escherichia coli.Wurgler S.M., Richardson C.C.Proc. Natl. Acad. Sci. U.S.A. 87:2740-2744(1990) The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase.Lipinska B., Zylicz M., Georgopoulos C.J. Bacteriol. 172:1791-1797(1990) Protein identification with N and C-terminal sequence tags in proteome projects.Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.J. Mol. Biol. 278:599-608(1998) Protease Do is essential for survival of Escherichia coli at high temperatures its identity with the htrA gene product.Seol J.H., Woo S.K., Jung E.M., Yoo S.J., Lee C.S., Kim K.J., Tanaka K., Ichihara A., Ha D.B., Chung C.H.Biochem. Biophys. Res. Commun. 176:730-736(1991) Site-directed mutagenesis of the HtrA (DegP) serine protease, whose proteolytic activity is indispensable for Escherichia coli survival at elevated temperatures (above 42 degrees Celsius) .Skorko-Glonek J., Wawrzynow A., Krzewski K., Kurpierz K., Lipinska B.Gene 163:47-52(1995) The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP.Danese P.N., Snyder W.B., Cosma C.L., Davis L.J., Silhavy T.J.Genes Dev. 9:387-398(1995) Comparison of the structure of wild-type HtrA heat shock protease and mutant HtrA proteins. A Fourier transform infrared spectroscopic study.Skorko-Glonek J., Krzewski K., Lipinska B., Bertoli E., Tanfani F.J. Biol. Chem. 270:11140-11146(1995) The DegP and DegQ periplasmic endoproteases of Escherichia coli specificity for cleavage sites and substrate conformation.Kolmar H., Waller P.R., Sauer R.T.J. Bacteriol. 178:5925-5929(1996) HtrA heat shock protease interacts with phospholipid membranes and undergoes conformational changes.Skorko-Glonek J., Lipinska B., Krzewski K., Zolese G., Bertoli E., Tanfani F.J. Biol. Chem. 272:8974-8982(1997) A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.Spiess C., Beil A., Ehrmann M.Cell 97:339-347(1999) Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate the PapA pilin.Jones C.H., Dexter P., Evans A.K., Liu C., Hultgren S.J., Hruby D.E.J. Bacteriol. 184:5762-5771(2002) The N-terminal region of HtrA heat shock protease from Escherichia coli is essential for stabilization of HtrA primary structure and maintaining of its oligomeric structure.Skorko-Glonek J., Zurawa D., Tanfani F., Scire A., Wawrzynow A., Narkiewicz J., Bertoli E., Lipinska B.Biochim. Biophys. Acta 1649:171-182(2003) Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins.Krojer T., Pangerl K., Kurt J., Sawa J., Stingl C., Mechtler K., Huber R., Ehrmann M., Clausen T.Proc. Natl. Acad. Sci. U.S.A. 105:7702-7707(2008) Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins.Jiang J., Zhang X., Chen Y., Wu Y., Zhou Z.H., Chang Z., Sui S.F.Proc. Natl. Acad. Sci. U.S.A. 105:11939-11944(2008) The role of the L2 loop in the regulation and maintaining the proteolytic activity of HtrA (DegP) protein from Escherichia coli.Sobiecka-Szkatula A., Gieldon A., Scire A., Tanfani F., Figaj D., Koper T., Ciarkowski J., Lipinska B., Skorko-Glonek J.Arch. Biochem. Biophys. 500:123-130(2010) Factors defining the functional oligomeric state of Escherichia coli DegP protease.Iwanczyk J., Leong V., Ortega J.PLoS ONE 6:E18944-E18944(2011) Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine.Krojer T., Garrido-Franco M., Huber R., Ehrmann M., Clausen T.Nature 416:455-459(2002) Roles of DegP in prevention of protein misfolding in the periplasm upon overexpression of penicillin acylase in Escherichia coli.Pan K.L., Hsiao H.C., Weng C.L., Wu M.S., Chou C.P.J. Bacteriol. 185:3020-3030(2003) Structural basis for the regulated protease and chaperone function of DegP.Krojer T., Sawa J., Schafer E., Saibil H.R., Ehrmann M., Clausen T.Nature 453:885-890(2008) HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues.Krojer T., Sawa J., Huber R., Clausen T.Nat. Struct. Mol. Biol. 17:844-852(2010) Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages.Kim S., Grant R.A., Sauer R.T.Cell 145:67-78(2011)

Other Notes

Small volumes of degP recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for degP purchase

MBS1198532 is a recombinant protein targeting degP. Also known as Recombinant Escherichia coli Periplasmic serine endoprotease DegP. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for degP. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
GenBank Nucleotide #
NCBI Official Full Name
serine endoprotease (protease Do), membrane-associated
NCBI Official Symbol
degP
NCBI Official Synonym Symbols
ECK0160; htrA; JW0157; ptd
UniProt Protein Name
Periplasmic serine endoprotease DegP
UniProt Synonym Protein Names
Heat shock protein DegP; Protease Do
UniProt Gene Name
degP
UniProt Synonym Gene Names
htrA; ptd
UniProt Entry Name
DEGP_ECOLI
NCBI Protein Information
serine endoprotease (protease Do), membrane-associated

NCBI Summary for degP

Autocleavage occurs after Cys95(Cys69 of mature form) or Gln108 (Gln82 of mature form). [More information is available at EcoGene: EG10463]. Protease Do, or DegP, is a periplasmic serine protease required for survival at high temperatures . [More information is available at EcoCyc: EG10463].

UniProt Comments for degP

DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures (PubMed:10319814). Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions (PubMed:16303867). DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids (PubMed:8830688). Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins (PubMed:8830688). Its proteolytic activity is essential for the survival of cells at elevated temperatures (PubMed:7557477). It can degrade IciA, Ada, casein, globin and PapA. DegP shares specificity with DegQ (PubMed:8830688). DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP).
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Precautions

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Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

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