Enterotoxin type E (entE) Recombinant Protein | entE recombinant protein

Recombinant Staphylococcus aureus Enterotoxin type E (entE)

Cat. Num. AAA1250406

• Gene Names: def; ECK3273; fms; JW3248
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Enterotoxin type E (entE); Recombinant Staphylococcus aureus Enterotoxin type E (entE); Polypeptide deformylase; entE recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 2-169aa; Full Length of Mature Protein
• Sequence: SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYAEEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEKSGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFELEADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEKLDRLKARA
• Sequence Length: 169

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-Page

Related Product Information for entE recombinant protein

Roves the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.

References

Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation.Mazel D., Pochet S., Marliere P.EMBO J. 13:914-923(1994) Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli.Guillon J.-M., Mechulam Y., Schmitter J.-M., Blanquet S., Fayat G.J. Bacteriol. 174:4294-4301(1992) 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) The Escherichia coli fmt gene, encoding methionyl-tRNA(fMet) formyltransferase, escapes metabolic control.Meinnel T., Guillon J.-M., Mechulam Y., Blanquet S.J. Bacteriol. 175:993-1000(1993) Enzymatic properties of Escherichia coli peptide deformylase.Meinnel T., Blanquet S.J. Bacteriol. 177:1883-1887(1995) Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site.Groche D., Becker A., Schlichting I., Kabsch W., Schultz S., Wagner A.F.Biochem. Biophys. Res. Commun. 246:342-346(1998) A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase.Meinnel T., Blanquet S., Dardel F.J. Mol. Biol. 262:375-386(1996) Solution structure of nickel-peptide deformylase.Dardel F., Ragusa S., Lazennec C., Blanquet S., Meinnel T.J. Mol. Biol. 280:501-513(1998) Crystal structure of the Escherichia coli peptide deformylase.Chan M.K., Gong W., Rajagopalan P.T.R., Hao B., Tsai C.M., Pei D.Biochemistry 36:13904-13909(1997) ErratumChan M.K., Gong W., Rajagopalan P.T.R., Hao B., Tsai C.M., Pei D.Biochemistry 37:13042-13042(1998) Structure of peptide deformylase and identification of the substrate binding site.Becker A., Schlichting I., Kabsch W., Schultz S., Wagner A.F.J. Biol. Chem. 273:11413-11416(1998) Iron center, substrate recognition and mechanism of peptide deformylase.Becker A., Schlichting I., Kabsch W., Groche D., Schultz S., Wagner A.F.Nat. Struct. Biol. 5:1053-1058(1998) Structural basis for the design of antibiotics targeting peptide deformylase.Hao B., Gong W., Rajagopalan P.T.R., Zhou Y., Pei D., Chan M.K.Biochemistry 38:4712-4719(1999)

NCBI and Uniprot Product Information

• NCBI GI #: 16131166
• NCBI GeneID: 947780
• NCBI Accession #: NP_417745.1
• NCBI GenBank Nucleotide #: NC_000913.3
• UniProt Accession #: P0A6K3; P27251; Q2M6V1; CAA54826
• Molecular Weight: 35.2 kDa
• NCBI Official Full Name: peptide deformylase
• NCBI Official Symbol: def
• NCBI Official Synonym Symbols: ECK3273; fms; JW3248
• NCBI Protein Information: peptide deformylase
• UniProt Protein Name: Peptide deformylase
• Protein Family: Enterotoxin
• UniProt Gene Name: def
• UniProt Synonym Gene Names: fms; PDF
• UniProt Entry Name: DEF_ECOLI

NCBI Description

The def gene is essential unless the fmt formylase gene is also inactivated. [More information is available at EcoGene: EG11440]. Peptide deformylase releases the formyl group from the amino terminal methionine residue of most nascent proteins . [More information is available at EcoCyc: EG11440].

Uniprot Description

Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.