protein

Beta-lactamase TEM/Bla Protein, E.coli (P.pastoris, His)

HY-P71804

5 μg;10 μg;50 μg

145;245;680 USD

Beta-lactamase TEM/Bla Protein, E.coli (P.pastoris, His)

proteins

P. pastoris

5 μg;10 μg;50 μg

145;245;680 USD

The β-lactamase TEM/Bla proteome is dominant in Enterobacteriaceae and hydrolyzes β-lactam bonds in β-lactam antibiotics, thereby conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 hydrolyze cefotaxime and ceftazidime, TEM-5 targets ceftazidime, and TEM-6 includes aztreonam. Beta-lactamase TEM/Bla Protein, E.coli (P.pastoris, His) is the recombinant E. coli-derived Beta-lactamase TEM/Bla protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of Beta-lactamase TEM/Bla Protein, E.coli (P.pastoris, His) is 263 a.a., with molecular weight of ~30.9 kDa.

E.coli

The Beta-lactamase TEM/Bla protein group stands out as the predominant class of beta-lactamases in enterobacteria, exerting their resistance mechanism by hydrolyzing the beta-lactam bond in susceptible beta-lactam antibiotics. This enzymatic activity imparts resistance specifically to penicillins and cephalosporins. Among the TEM variants, TEM-3 and TEM-4 demonstrate the ability to hydrolyze cefotaxime and ceftazidime, while TEM-5 targets ceftazidime. TEM-6 extends its hydrolyzing capability to ceftazidime and aztreonam. Notably, TEM-8/CAZ-2, TEM-16/CAZ-7, and TEM-24/CAZ-6 exhibit marked activity against ceftazidime. Additionally, IRT-4 showcases resistance to beta-lactamase inhibitors, highlighting the diverse enzymatic profiles within the TEM/Bla protein family, crucial in the context of antibiotic resistance in clinical settings.

bla; blaT-3; blaT-4; blaT-5; TEM-1; TEM-16/CAZ-7; TEM-2; TEM-24/CAZ-6; TEM-3; TEM-4; TEM-5; TEM-6; TEM-8/CAZ-2

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized after extensive dialysis against solution in PBS, 6% Trehalose, pH 7.4.

Room temperature in continental US; may vary elsewhere.