β lactamase production nitrocefin discs  (Millipore)


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  • 94
    Name:
    Nitrocefin disks
    Description:
    Nitrocefin is a chromogenic cephalosporin it has a characteristic beta lactam ring which on oxidation by beta lactamase renders nitrocefin from yellow to red in color It is light sensitive in nature and is quite expensive It is used for the rapid detection of beta lactamase enzymes in isolated colonies of Neisseria gonorrhoeae Moraxella catarrhalis Staphylococcus spp Haemophilus influenzae and anaerobic bacteria
    Catalog Number:
    49862
    Price:
    None
    Applications:
    For the rapid detection of beta-lactamase enzymes in isolated colonies of Neisseria gonorrhoeae, Moraxella catarrhalis, Staphylococcus spp., Haemophilus influenzae and anaerobic bacteria.
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    Structured Review

    Millipore β lactamase production nitrocefin discs
    Nitrocefin is a chromogenic cephalosporin it has a characteristic beta lactam ring which on oxidation by beta lactamase renders nitrocefin from yellow to red in color It is light sensitive in nature and is quite expensive It is used for the rapid detection of beta lactamase enzymes in isolated colonies of Neisseria gonorrhoeae Moraxella catarrhalis Staphylococcus spp Haemophilus influenzae and anaerobic bacteria
    https://www.bioz.com/result/β lactamase production nitrocefin discs/product/Millipore
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    β lactamase production nitrocefin discs - by Bioz Stars, 2020-09
    94/100 stars

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    Related Articles

    Functional Assay:

    Article Title: Evidence for a purifying selection acting on the ?-lactamase locus in epidemic clones of methicillin-resistant Staphylococcus aureus
    Article Snippet: .. The presence of a functional β-lactamase locus was confirmed by nitrocefin disks (Sigma) for all strains, in the presence and absence of an inducer (oxacillin at 0.05 mg/L). ..

    Article Title: Methicillin-Resistance in Staphylococcus aureus Is Not Affected by the Overexpression in Trans of the mecA Gene Repressor: A Surprising Observation
    Article Snippet: .. β-lactamase detection Detection of functional β-lactamase locus was performed either with BBL™ DrySlide™ Nitrocefin (BD) (strains listed in ) or with nitrocefin disks (Sigma-Aldrich) (strains listed in ) according to the manufacturer's recommendations for cultures grown overnight in TSB with and without induction with oxacillin at 0.5 µg/ml. .. In the case of strains negative for the Nitrocefin assay, the absence of β-lactamase genes was confirmed by PCR with three pairs of primers targeting internal fragments of ca.

    other:

    Article Title: Comparison of Effects of Medium Composition and Atmospheric Conditions on Detection of Bilophila wadsworthia ?-Lactamase by Cefinase and Cefinase Plus Methods
    Article Snippet: Cefinase, Cefinase Plus, and penicillin (2-U) disks were obtained from BBL Microbiology Systems, and triphenyltetrazolium chloride was obtained from Sigma Chemical Co. Ampicillin (Pfizer Inc., New York, N.Y.), penicillin G (Eli Lilly and Company, Indianapolis, Ind.), and sulbactam (Pfizer) were obtained from the manufacturers and prepared by the methods outlined in the National Committee for Clinical Laboratory Standards (NCCLS) reference method ( ).

    Article Title: Structural and Regulatory Changes in PBP4 Trigger Decreased β-Lactam Susceptibility in Enterococcus faecalis
    Article Snippet: Testing for the presence of β-lactamase was carried out with nitrocefin disks (Sigma-Aldrich) in accordance with the manufacturer’s instructions.

    Article Title: Co-carriage of Staphylococcus aureus, Streptococcus pneumoniae, Haemophilus influenzae and Moraxella catarrhalis among three different age categories of children in Hungary
    Article Snippet: Nitrocefin disks (Sigma-Aldrich, St. Louis, USA) were used to detect β-lactamase production of ampicillin resistant H . influenzae isolates.

    Article Title: Cross-feeding modulates antibiotic tolerance in bacterial communities
    Article Snippet: Nitrocefin discs (Sigma-Aldrich, 49862) were used to determine if M. extorquens was producing a β-lactamase.

    Article Title: Cross-feeding modulates antibiotic tolerance in bacterial communities
    Article Snippet: Testing β-lactamase production Nitrocefin discs (Sigma-Aldrich, 49862) were used to determine if M. extorquens was producing a β-lactamase.

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  • 97
    Millipore nitrocefin
    Vasna and Vasnb specifically and directly bind Islr2 with low affinity. a . Identification of the Vasnb-Islr2 interaction using the AVEXIS assay. Vasnb interacted with Islr2 and no other protein when presented either as bait against 194 prey ectodomains (upper panel) or as prey against 149 baits (lower panel). Statistical threshold (dashed lines) is calculated as 3 standard deviations over the mean. b . Quantification of the interaction between Vasna and Islr2 using surface plasmon resonance. Upper panel: Serial dilutions of purified monomeric Islr2-Cd4d3+4-6xHis were sequentially injected until binding equilibrium was reached over flow cells in which biotinylated Vasna ectodomains were immobilized on a streptavidin-coated sensor chip at high (solid line) and low (dashed line) levels. An equilibrium binding constant ( K D ) of 12.4 μM was calculated by non-linear curve fitting to both binding curves. Lower panel: kinetic analysis of the Vasna-Islr2 interaction. A dissociation rate constant ( k off ) was calculated by globally fitting a first order decay curve to the dissociation phase of three concentrations (7 μM, 14 μM, 28 μM) of Islr2-Cd4d3+4-6xHis; the interaction half-life (t 1/2 ) was calculated as t 1/2 = ln2/ k off . Each data point represents average values from normalized dissociation data (error bars = ± 1 standard deviation, n = 3). Control dissociation measurements (dashed line) are from 28 μM Islr2-Cd4d3+4-6xHis injected over a flow cell containing the Cd4d3+4 tag alone. c . AVEXIS screening to identify the extracellular domains mediating the interaction between Vasna and Islr2. We observed <t>nitrocefin</t> hydrolysis whenever the EGF domain of Vasna could bind to the LRR domain of Islr2. Conversely, the truncated LRR domain encoded by islr2 sa82 did not show activity, indicating that the zebrafish mutant allele is functionally null. d . Schematic model for the interaction between Vasorin and Islr2, where the proteins bind in trans , a property suggested by the non-overlapping expression patterns of the two genes
    Nitrocefin, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nitrocefin/product/Millipore
    Average 97 stars, based on 11 article reviews
    Price from $9.99 to $1999.99
    nitrocefin - by Bioz Stars, 2020-09
    97/100 stars
      Buy from Supplier

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    Vasna and Vasnb specifically and directly bind Islr2 with low affinity. a . Identification of the Vasnb-Islr2 interaction using the AVEXIS assay. Vasnb interacted with Islr2 and no other protein when presented either as bait against 194 prey ectodomains (upper panel) or as prey against 149 baits (lower panel). Statistical threshold (dashed lines) is calculated as 3 standard deviations over the mean. b . Quantification of the interaction between Vasna and Islr2 using surface plasmon resonance. Upper panel: Serial dilutions of purified monomeric Islr2-Cd4d3+4-6xHis were sequentially injected until binding equilibrium was reached over flow cells in which biotinylated Vasna ectodomains were immobilized on a streptavidin-coated sensor chip at high (solid line) and low (dashed line) levels. An equilibrium binding constant ( K D ) of 12.4 μM was calculated by non-linear curve fitting to both binding curves. Lower panel: kinetic analysis of the Vasna-Islr2 interaction. A dissociation rate constant ( k off ) was calculated by globally fitting a first order decay curve to the dissociation phase of three concentrations (7 μM, 14 μM, 28 μM) of Islr2-Cd4d3+4-6xHis; the interaction half-life (t 1/2 ) was calculated as t 1/2 = ln2/ k off . Each data point represents average values from normalized dissociation data (error bars = ± 1 standard deviation, n = 3). Control dissociation measurements (dashed line) are from 28 μM Islr2-Cd4d3+4-6xHis injected over a flow cell containing the Cd4d3+4 tag alone. c . AVEXIS screening to identify the extracellular domains mediating the interaction between Vasna and Islr2. We observed nitrocefin hydrolysis whenever the EGF domain of Vasna could bind to the LRR domain of Islr2. Conversely, the truncated LRR domain encoded by islr2 sa82 did not show activity, indicating that the zebrafish mutant allele is functionally null. d . Schematic model for the interaction between Vasorin and Islr2, where the proteins bind in trans , a property suggested by the non-overlapping expression patterns of the two genes

    Journal: Neural Development

    Article Title: The LRR receptor Islr2 is required for retinal axon routing at the vertebrate optic chiasm

    doi: 10.1186/s13064-015-0050-x

    Figure Lengend Snippet: Vasna and Vasnb specifically and directly bind Islr2 with low affinity. a . Identification of the Vasnb-Islr2 interaction using the AVEXIS assay. Vasnb interacted with Islr2 and no other protein when presented either as bait against 194 prey ectodomains (upper panel) or as prey against 149 baits (lower panel). Statistical threshold (dashed lines) is calculated as 3 standard deviations over the mean. b . Quantification of the interaction between Vasna and Islr2 using surface plasmon resonance. Upper panel: Serial dilutions of purified monomeric Islr2-Cd4d3+4-6xHis were sequentially injected until binding equilibrium was reached over flow cells in which biotinylated Vasna ectodomains were immobilized on a streptavidin-coated sensor chip at high (solid line) and low (dashed line) levels. An equilibrium binding constant ( K D ) of 12.4 μM was calculated by non-linear curve fitting to both binding curves. Lower panel: kinetic analysis of the Vasna-Islr2 interaction. A dissociation rate constant ( k off ) was calculated by globally fitting a first order decay curve to the dissociation phase of three concentrations (7 μM, 14 μM, 28 μM) of Islr2-Cd4d3+4-6xHis; the interaction half-life (t 1/2 ) was calculated as t 1/2 = ln2/ k off . Each data point represents average values from normalized dissociation data (error bars = ± 1 standard deviation, n = 3). Control dissociation measurements (dashed line) are from 28 μM Islr2-Cd4d3+4-6xHis injected over a flow cell containing the Cd4d3+4 tag alone. c . AVEXIS screening to identify the extracellular domains mediating the interaction between Vasna and Islr2. We observed nitrocefin hydrolysis whenever the EGF domain of Vasna could bind to the LRR domain of Islr2. Conversely, the truncated LRR domain encoded by islr2 sa82 did not show activity, indicating that the zebrafish mutant allele is functionally null. d . Schematic model for the interaction between Vasorin and Islr2, where the proteins bind in trans , a property suggested by the non-overlapping expression patterns of the two genes

    Article Snippet: In order to reveal binding events, 50 μl of 100 μg/ml nitrocefin (a beta-lactamase substrate; 484400, Calbiochem) was added.

    Techniques: SPR Assay, Purification, Injection, Binding Assay, Flow Cytometry, Chromatin Immunoprecipitation, Standard Deviation, Activity Assay, Mutagenesis, Expressing