CENTA β-Lactamase Substrate

<strong>CENTA β-Lactamase Substrate</strong>_x000D_ <strong>Catalog number:</strong> B2014174_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 5 mg_x000D_ <strong>Molecular Weight or Concentration:</strong> 535.57 g/mol_x000D_ <strong>Supplied as:</strong> Powder_x000D_ <strong>Applications:</strong> molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> -20°C_x000D_ <strong>Keywords:</strong> CENTA β-Lactamase Substrate_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity &gt;18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Jones RN, Wilson HW, Novick WJ Jr, Barry AL, Thornsberry C. In vitro evaluation of CENTA, a new beta-lactamase-susceptible chromogenic cephalosporin reagent J Clin Microbiol. 1982 May;15(5):954-8._x000D_ 2: Shrivastav A, Sharma RK, Shrivastava N, Gautam V, Jain SK. Study of inhibitory potential and percent inhibition of oil of Syzygium aromaticum and leaves of Ocimum sanctum on ESBL enzyme from Escherichia coli in broilers of Jabalpur Indian J Pharmacol. 2019 Sep-Oct;51(5):337-342._x000D_ 3: Raczynska JE, Imiolczyk B, Komorowska M, Sliwiak J, Czyrko-Horczak J, Brzezinski K, Jaskolski M. Flexible loops of New Delhi metallo-_-lactamase modulate its activity towards different substrates Int J Biol Macromol. 2020 Apr 28;158:104-115._x000D_ 4: Mikhnevich TA, Vyatkina Turkova AV, Grigorenko VG, Rubtsova MY, Rukhovich GD, Letarova MA, Kravtsova DS, Vladimirov SA, Orlov AA, Nikolaev EN, Zherebker A, Perminova IV. Inhibition of Class A _-Lactamase (TEM-1) by Narrow Fractions of Humic Substances ACS Omega. 2021 Sep 7;6(37):23873-23883._x000D_ 5: Mandal S, Maharjan M, Ganguly S, Chatterjee M, Singh S, Buckner FS, Madhubala R. High-throughput screening of amastigotes of Leishmania donovani clinical isolates against drugs using a colorimetric beta-lactamase assay Indian J Exp Biol. 2009 Jun;47(6):475-9._x000D_ 6: van Berkel SS, Brem J, Rydzik AM, Salimraj R, Cain R, Verma A, Owens RJ, Fishwick CW, Spencer J, Schofield CJ. Assay platform for clinically relevant metallo-_-lactamases J Med Chem. 2013 Sep 12;56(17):6945-53._x000D_ 7: Vella P, Hussein WM, Leung EW, Clayton D, Ollis DL, Miti N, Schenk G, McGeary RP. The identification of new metallo-_-lactamase inhibitor leads from fragment-based screening Bioorg Med Chem Lett. 2011 Jun 1;21(11):3282-5._x000D_ 8: Bebrone C, Moali C, Mahy F, Rival S, Docquier JD, Rossolini GM, Fastrez J, Pratt RF, Frre JM, Galleni M. CENTA as a chromogenic substrate for studying beta-lactamases Antimicrob Agents Chemother. 2001 Jun;45(6):1868-71._x000D_ 9: Morin S, Clouthier CM, Gobeil S, Pelletier JN, Gagn SM. Backbone resonance assignments of an artificially engineered TEM-1/PSE-4 Class A _-lactamase chimera Biomol NMR Assign. 2010 Oct;4(2):127-30._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/29321962">10: Grigorenko V, Uporov I, Rubtsova M, Andreeva I, Shcherbinin D, Veselovsky A, Serova O, Ulyashova M, Ishtubaev I, Egorov A. Mutual influence of secondary and key drug-resistance mutations on catalytic properties and thermal stability of TEM-type _-lactamases FEBS Open Bio. 2017 Dec 11;8(1):117-129. </a>_x000D_ _x000D_ <strong>Products Related to CENTA β-Lactamase Substrate can be found at</strong> <a href="https://moleculardepot.com/product-category/Substrates/"> Substrates</a>