SKU: N005  / 
    CAS Number: 41906-86-9


    $154.00 - $966.50

    Nitrocefin is a chromogenic cephalosporin used to detect β-lactamases produced by β-lactam resistant bacteria. It does not appear to have antimicrobial properties, but has useful diagnostic properties.  It can be used as a reagent in β-lactamase activity studies.  Nitrocefin is soluble in DMSO.

    Application Nitrocefin is useful for the detection of β-lactamase patterns from bacterial cell extracts by isoelectric focusing. It can also be used in biosensor development and protein switch technology.
    Mechanism of Action β-lactamases hydrolyze the amide bond between the carbonyl carbon and the nitrogen in the β-lactam ring of Nitrocefin. Intact Nitrocefin is converted to hydrolyzed Nitrocefin under visible light (~ 380-500 nm) and a color change occurs from yellow (max at pH 7.0 = 390 nm) to red (max at pH 7.0 = 486 nm).
    Microbiology Applications Nitrocefin is used to detect β-lactamase activity from suspected β-lactam resistant bacteria (see Protocol).  It is commonly used at a working concentration of 0.5 - 1.0 mg/ml.
    Molecular Formula C21H16N4O8S2

    Nitrocefin (TOKU-E) was used to study:

    TEM-1 ß-lactamase activity:
    "Label-free measurements of reaction kinetics using a droplet-based optofluidic device." Zhangming et al.  See Link.

    Biosensor development: 
    "Parts-per-million of polyethylene glycol as a non-interfering blocking agent for homogeneous biosensor development." Liu et al.  See Link.

    Surrogate ß-lactamase-nitrocefin assay: 
    "A cell-free fluorometric high-throughput screen for inhibitors of Rtt109-catalyzed histone acetylation." Dahlin et al. See Link.

    EstG34 ß-lactamases:
    "An unusual feruloyl esterase belonging to family VIII esterases and displaying a broad substrate range" Ohlhoff et al.  See Link.

    VIM-2 Metallo-ß-lactamases (MBLs):
     "Inhibiting the VIM-2 Metallo-ß-Lactamase by graphene oxide and carbon nanotubes." Huang et al. See Link.

    ß-lactamase production in E. coli and Klebsiella species:
    "Occurrence of beta-lactamases and the antibiogram pattern of clinical isolates of Escherichia coli and Klebsiella species in Nsukka metropolis." Eze E et al.  See Link.

    Engineered protein switches:
     "Electrochemical activation of engineered protein switches." Choi et al.  See Link.

    ß-lactamases (various):
    "Molecular determinants for protein stabilization by insertional fusion to a thermophilic host protein." Pierre et al. See Link.

    Enzymatic protein switches:
    "Enzymatic protein switches built from paralogous input domains."  Tullman and Nicholes.  See Link.

    Guntas G, Mitchell S and Ostermeier M (2004)  A molecular switch created by in vitro recombination of nonhomologous genes. Cell Press 11(11):1483-1487

    O'Callaghan CH et al (1972)  Novel method for detection of B-Lactamases by using a chromogenic cephalosporin substrate. Antimicrob. Agents. Chemother. 1(4):283-288

    Parr, TR et al (1984)  Simple screening method for beta-lactamase-positive and-negative Ampicillin-resistant Haemophilus Influenzae isolates.  J. Clin. Microbiol.  20(1):131-132