Recombinant Escherichia coli (strain K12) Protease 7 | MyBioSource MBS1147844 product information

product summary

company name :

MyBioSource

product type :

protein

product name :

Recombinant Escherichia coli (strain K12) Protease 7

catalog :

MBS1147844

quantity :

0.05 mg (E-Coli)

price :

190 USD

more info or order :

MyBioSource product webpage

product information

catalog number :

MBS1147844

products type :

Recombinant Protein

products full name :

Recombinant Escherichia coli (strain K12) Protease 7

products short name :

Protease 7

products name syn :

Omptin; Outer membrane protein 3B; Protease A; Protease VII

other names :

DLP12 prophage; outer membrane protease VII; outer membrane protein 3b; Protease 7; DLP12 prophage; outer membrane protease VII; outer membrane protein 3b; Omptin; Outer membrane protein 3B; Protease A; Protease VII

products gene name :

ompT

other gene names :

ompT; ompT; ECK0557; JW0554

uniprot entry name :

OMPT_ECOLI

host :

E Coli or Yeast or Baculovirus or Mammalian Cell

sequence positions :

21-317; Mature full length protein

sequence length :

317

sequence :

STETLSFTPDNINADISLGTLSGKTKERVYLAEEGGRKV
SQLDWKFNNAAIIKGAINWDLMPQISIGAAGWTTLGSRG
GNMVDQDWMDSSNPGTWTDESRHPDTQLNYANEFDLNIK
GWLLNEPNYRLGLMAGYQESRYSFTARGGSYIYSSEEGF
RDDIGSFPNGERAIGYKQRFKMPYIGLTGSYRYEDFELG
GTFKYSGWVESSDNDEHYDPGKRITYRSKVKDQNYYSVA
VNAGYYVTPNAKVYVEGAWNRVTNKKGNTSLYDHNNNTS
DYSKNGAGIENYNFITTAGLKYTF

purity :

Greater than 90% as determined by SDS-PAGE.

form :

Liquid containing glycerol; lyophilization may be available upon request.

storage stability :

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

products description :

Protease that can cleave T7 RNA polymerase, ferric enterobactin receptor protein (FEP), antimicrobial peptide protamine and other proteins. This protease has a specificity for paired basic residues.

products references :

Complete nucleotide sequence and deduced amino acid sequence of the ompT gene of Escherichia coli K-12.Grodberg J., Lundrigan M.D., Toledo D.L., Mangel W.F., Dunn J.J.Nucleic Acids Res. 16:1209-1209(1988) Purification, characterization, and primary structure of Escherichia coli protease VII with specificity for paired basic residues identity of protease VII and OmpT.Sugimura K., Nisihihara T.J. Bacteriol. 170:5625-5632(1988) 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) A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.DNA Res. 3:137-155(1996) Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis.Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M., Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.Electrophoresis 19:837-844(1998) Identification of OmpT as the protease that hydrolyzes the antimicrobial peptide protamine before it enters growing cells of Escherichia coli.Stumpe S., Schmid R., Stephens D.L., Georgiou G., Bakker E.P.J. Bacteriol. 180:4002-4006(1998) In vitro folding, purification and characterization of Escherichia coli outer membrane protease ompT.Kramer R.A., Zandwijken D., Egmond M.R., Dekker N.Eur. J. Biochem. 267:885-893(2000) Identification of essential acidic residues of outer membrane protease OmpT supports a novel active site.Kramer R.A., Vandeputte-Rutten L., de Roon G.J., Gros P., Dekker N., Egmond M.R.FEBS Lett. 505:426-430(2001) Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site.Vandeputte-Rutten L., Kramer R.A., Kroon J., Dekker N., Egmond M.R., Gros P.EMBO J. 20:5033-5039(2001)

ncbi gi num :

16128548

ncbi acc num :

NP_415097.1

ncbi gb acc num :

NC_000913.3

uniprot acc num :

P09169

ncbi mol weight :

37.6kD

ncbi summary :

Mg(2+) stimulon-PhoPQ regulon, EvgAS-PhoPQ cascade enhanced-expression subset. [More information is available at EcoGene: EG10673]. OmpT is an outer membrane protease with specificity for paired basic residues ; detailed studies on substrate specificity have been performed . [More information is available at EcoCyc: EG10673].

size1 :

0.05 mg (E-Coli)

price1 :

190 USD

size2 :

0.2 mg (E-Coli)

price2 :

460

size3 :

0.5 mg (E-Coli)

price3 :

750

size4 :

0.05 mg (Baculovirus)

price4 :

950

size5 :

0.05 mg (Mammalian-Cell)

price5 :

1170

more info or order :

MyBioSource product webpage