Luciferase (bacterial)
Based on 1 Customer Validation
Luciferase (bacterial) acts as a luminescence inducer and catalyst. Luciferase (bacterial) catalyzes the reduction of methylene blue, quinones, ferricyanide, and FMN using reduced DPN (HY-12452) (or an alternative electron donor for FMN). Luciferase (bacterial) binds to reduced FMN to form a luminescent reaction complex. Luciferase (bacterial) scavenges reactive oxygen species (ROS) and protects bacterial cells from oxidative stress damage. Luciferase (bacterial) is applicable to studies related to oxidative stress.
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- CAS No.: 9014-00-0
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보관:
Please store the product under the recommended conditions in the Certificate of Analysis.
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Biological Activity
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Chemical Information
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용액&용해도
- 순도&문서
- References
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Help & FAQs
Biological Activity
제품 설명
In Vitro
Luciferase (bacterial) protects Vibrio harveyi luxA and luxB mutant cells against oxidative stress induced by 1.25 mM hydrogen peroxide, 0.14 mM cumene hydroperoxide, 0.3 mM t-butyl hydroperoxide, and 0.2 mM ferrous sulfate[2].
Luciferase (bacterial) catalyzes oxygen-dependent luminescence requiring reduced FMN and long-chain aldehyde, with reduced FMN binding to the enzyme via two sites (dissociation constants K1 = 3.72×10-6 M and K2 = 2.69×10-6 M), and supports luminescence with DPNH or TPNH when FMN is present, while aldehyde concentration directly determines total light output[1].
Luciferase (bacterial) catalyzes metal-independent oxidation of DPNH by ferricyanide, Methylene blue (HY-14536), and quinones in the absence of aldehyde and FMN, with ferricyanide competing with FMN for a reduced enzyme intermediate to suppress luminescence until fully reduced[1].
Luciferase (bacterial) exhibits species-specific differences in FMNH2 binding affinity and C4a-(hydro)peroxyflavin formation rates, with V. campbellii Lux displaying the highest FMNH2 binding affinity (Kd = 1.8 μM) and fastest oxygen reaction rate (253 s-1 at 0.26 mM oxygen)[3].
Luciferase (bacterial) (4-27 μM) binds aldehyde at two distinct sites, with high-affinity binding acting as a substrate interaction and lower-affinity binding at higher concentrations inhibiting catalytic activity by blocking FMNH2 binding and reducing C4a-(hydro)peroxyflavin formation[3].
Luciferase (bacterial) has specific active site and flexible loop residues critical for catalytic activity, intermediate stability, and light emission properties; mutations to these residues reduce bioluminescence efficiency, alter intermediate decay rates, or shift emission spectra[3].
Luciferase (bacterial) binds FMNH2 with an apparent Kd of 0.08 μM at room temperature, with initial bioluminescence intensity proportional to FMNH2 concentration and exponential first-order decay kinetics[5].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
Chemical Information
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CAS No. 9014-00-0
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Appearance Solid
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Color White to light yellow
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SMILES
[Luciferase (bacterial)]
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Structure Classification
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Initial Source
Neonothopanus nambi fungus
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선적
Room temperature in continental US; may vary elsewhere.
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보관
Please store the product under the recommended conditions in the Certificate of Analysis.
용액&용해도
In Vitro:
H2O : 20 mg/mL (Need ultrasonic)
순도&문서
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Data Sheet (276 KB)
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SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
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Handling Instructions (2659 KB)
References
[2]. Szpilewska H, et al. Experimental evidence for the physiological role of bacterial luciferase in the protection of cells against oxidative stress. Current microbiology. 2003 Nov;47(5):379-82. [Content Brief]
[3]. Tinikul R, et al. Bacterial luciferase: Molecular mechanisms and applications. The Enzymes. 2020;47:427-455. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
Luciferase (bacterial) Related Classifications
HY-P1004 Related Classifications
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