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Tryptophanase

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Tryptophanase is a zymogen-converting enzyme and inducible enzyme that can convert its inactive precursor form into an active enzyme without additional polypeptide synthesis. In Escherichia coli K12, tryptophanase functions as an inducible enzyme, and its induction kinetics are similar to those of β-galactosidase. Tryptophanase catalyzes the conversion of L-tryptophan to indole.

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CAS No.: 9024-00-4

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Please store the product under the recommended conditions in the Certificate of Analysis.

Tryptophanase Chemical Structure

CAS No.: 9024-00-4

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Sample (0.1mg)

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(In Japan)

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Fluorescent Dye

Strong Fluorescence Signal / Multi-Disciplinary Applications / High Fluorescence Specificity

Activité biologique
- Description
- In Vitro
Chemical Information
Pureté et documentation
Références
Calculators
Help & FAQs
Bioz

Activité biologique

Description

In Vitro

Tryptophanase (1.5 × 10^-3 M L-tryptophan inducer; 100 μg/mL chloramphenicol; multiple time points) induction in Escherichia coli K12 strain C600 (F^-) has a 3-4 min lag phase post-inducer addition, with de novo synthesis capacity decaying with a half-life of 2.5 min after inducer removal; in phage-infected F^- cells, this half-life is 1.5 min, while in F⁺ cells it remains 2.5 min. A tryptophanase precursor accumulates starting 1-1.5 min post-induction, with conversion to active enzyme requiring 1-2 min^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

Chemical Information

CAS No. 9024-00-4
Appearance Solid
Color White to off-white
SMILES

[Tryptophanase]
Livraison

Room temperature in continental US; may vary elsewhere.
Stockage

Please store the product under the recommended conditions in the Certificate of Analysis.

Pureté et documentation

Select Batch:

Pureté: 99.98%

Assay: 99.98%

ee.: 99.98%

Fiche technique (265 KB)
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)
- Portuguese - PT (251 KB)
COA (2659 KB)
Elemental Analysis Report (2659 KB)
HNMR (2659 KB)
CNMR (2659 KB)
RP-HPLC (2659 KB)
NP-HPLC (2659 KB)
MS (2659 KB)
LCMS (2659 KB)
IR (2659 KB)
GC (2659 KB)
OR (2659 KB)
SDS-PAGE (2659 KB)
SEC-HPLC (2659 KB)
Other Report (2659 KB)
Instruction de manipulation (2659 KB)

Références

[1]. Bilezikian JP, et al. Mechanism of tryptophanase induction in Escherichia coli. J Mol Biol. 1967 Aug 14;27(3):495-506. [Content Brief]

Calculators

Calculateur de molarité

Mass (g) = Concentration (mol/L) × Volume (L) × Molecular Weight (g/mol)

Mass Mass

Concentration Concentration

Volume Volume

Molecular Weight Molecular Weight

Calculateur de dilution

Concentration _(start) × Volume _(start) = Concentration _(final) × Volume _(final)

Concentration _(start) Concentration _(start)

Volume _(start) Volume _(start)

Concentration _(final) Concentration _(final)

Volume _(final) Volume _(final)

Help & FAQs

How should lyophilized recombinant proteins be reconstituted and stored?

1. Before opening the cap, centrifuge the vial at 13000 rpm for 20-30 seconds. This step will ensure that any lyophilized powder that may have adhered to the cap or walls is collected at the bottom of the vial, minimizing the risk of product loss.

Keywords

100 mg

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