catalog number :
MBS1262737
products type :
Recombinant Protein
products full name :
Recombinant Escherichia coli Beta-lactamase TEM
products short name :
Beta-lactamase TEM
products name syn :
IRT-4; Penicillinase; TEM-1; TEM-16/CAZ-7; TEM-2; TEM-24/CAZ-6; TEM-3; TEM-4; TEM-5; TEM-6; TEM-8/CAZ-2
other names :
beta-lactamase (plasmid); Beta-lactamase TEM; beta-lactamase; IRT-4; Penicillinase; TEM-1; TEM-16/CAZ-7; TEM-2; TEM-24/CAZ-6; TEM-3; TEM-4; TEM-5; TEM-6; TEM-8/CAZ-2
other gene names :
pIGAL1_03; bla
uniprot entry name :
BLAT_ECOLX
host :
E Coli or Yeast or Baculovirus or Mammalian Cell
sequence positions :
24-286, Mature full length protein.
sequence :
HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEE
RFPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLV
EYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTI
GGPKELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTT
MPAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPL
LRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIV
VIYTTGSQATMDERNRQIAEIGASLIKHW
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 :
T-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. T-3 and T-4 are capable of hydrolyzing cefotaxime and ceftazidime. T-5 is capable of hydrolyzing ceftazidime. T-6 is capable of hydrolyzing ceftazidime and aztreonam. T-8/CAZ-2, T-16/CAZ-7 and T-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors.
products references :
Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322.Sutcliffe J.G.Proc. Natl. Acad. Sci. U.S.A. 75:3737-3741(1978)
Complete nucleotide sequence of the Escherichia coli plasmid pBR322.Sutcliffe J.G.Cold Spring Harb. Symp. Quant. Biol. 43:77-90(1979)
DNA replication of the resistance plasmid R100 and its control.Ohtsubo H., Ryder T.B., Maeda Y., Armstrong K., Ohtsubo E.Adv. Biophys. 21:115-133(1986)
Partial amino acid sequence of penicillinase coded by Escherichia coli plasmid R6K.Ambler R.P., Scott G.K.Proc. Natl. Acad. Sci. U.S.A. 75:3732-3736(1978)
The TEM-3 beta-lactamase, which hydrolyzes broad-spectrum cephalosporins, is derived from the TEM-2 penicillinase by two amino acid substitutions.Sougakoff W., Goussard S., Courvalin P.FEMS Microbiol. Lett. 56:343-348(1988)
A new example of physical linkage between Tn1 and Tn21
the antibiotic multiple-resistance region of plasmid pCFF04 encoding extended-spectrum beta-lactamase TEM-3.Mabilat C., Lourencao-Vital J., Goussard S., Courvalin P.Mol. Gen. Genet. 235:113-121(1992)
Characterization of the plasmid genes blaT-4 and blaT-5 which encode the broad-spectrum beta-lactamases TEM-4 and TEM-5 in enterobacteriaceae.Sougakoff W., Petit A., Goussard S., Sirot D., Bure A., Courvalin P.Gene 78:339-348(1989)
An IS1-like element is responsible for high-level synthesis of extended-spectrum beta-lactamase TEM-6 in Enterobacteriaceae.Goussard S., Sougakoff W., Mabilat C., Bauernfeind A., Courvalin P.J. Gen. Microbiol. 137:2681-2687(1991)
Nucleotide sequences of CAZ-2, CAZ-6, and CAZ-7 beta-lactamase genes.Chanal C., Poupart M.C., Sirot D., Labia R., Sirot J., Cluzel R.Antimicrob. Agents Chemother. 36:1817-1820(1992)
Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to beta-lactamase inhibitors.Brun T., Peduzzi J., Canica M.M., Paul G., Nevot P., Barthelemy M., Labia R.FEMS Microbiol. Lett. 120:111-117(1994)
Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5-A resolution.Jelsch C., Lenfant F., Masson J.-M., Samama J.-P.FEBS Lett. 299:135-142(1992)
Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8-A resolution.Jelsch C., Mourey L., Masson J.-M., Samama J.-P.Proteins 16:364-383(1993)
A potent new mode of beta-lactamase inhibition revealed by the 1.7 A X-ray crystallographic structure of the TEM-1-BLIP complex.Strynadka N.C.J., Jensen S.E., Alzari P.M., James M.N.G.Nat. Struct. Biol. 3:290-297(1996)
Crystal structure of an acylation transition-state analog of the TEM-1 beta-lactamase. Mechanistic implications for class A beta-lactamases.Maveyraud L., Pratt R.F., Samama J.-P.Biochemistry 37:2622-2628(1998)
X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1 beta-lactamase
direct observation of electrostatic modulation in resistance to inactivation by clavulanic acid.Swaren P., Golemi D., Cabantous S., Bulychev A., Maveyraud L., Mobashery S., Samama J.-P.Biochemistry 38:9570-9576(1999)
ncbi acc num :
NP_943295.1
ncbi gb acc num :
NC_005248.1
ncbi mol weight :
44.89kD