Periplasmic serine endoprotease DegP (degP), Escherichia coli, recombinant

Organism: Escherichia coli (strain K12). Source: Yeast. Expression Region: 27-474aa. Protein Length: Full Length of Mature Protein. Tag Info: N-terminal 6xHis-tagged. Target Protein 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. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. 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. Storage: 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. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: DegP acts as a chaperone at low tperatures but switches to a peptidase (heat shock protein) at higher tperatures. It degrades transiently denatured and unfolded 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 tperatures. 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-mbrane proteins (OMP). Reference: 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). Function: DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures