Description
ONPG is a colorimetric and spectrophotometric substrate for detection of β-galactosidase activity.
Product information
CAS Number: 369-07-3
Molecular Weight: 301.25
Formula: C12H15NO8
Synonym:
2-Nitrophenyl β-D-galactopyranoside
Chemical Name: (2R,3R,4S,5R,6S)-2-(hydroxymethyl)-6-(2-nitrophenoxy)oxane-3,4,5-triol
Smiles: OC[C@H]1O[C@@H](OC2=CC=CC=C2N(=O)=O)[C@H](O)[C@@H](O)[C@H]1O
InChiKey: KUWPCJHYPSUOFW-YBXAARCKSA-N
InChi: InChI=1S/C12H15NO8/c14-5-8-9(15)10(16)11(17)12(21-8)20-7-4-2-1-3-6(7)13(18)19/h1-4,8-12,14-17H,5H2/t8-,9+,10+,11-,12-/m1/s1
Technical Data
Appearance: Solid Power
Purity: ≥98% (or refer to the Certificate of Analysis)
Solubility: H2O : 7.4 mg/mL (24.56 mM; Need ultrasonic)
Shipping Condition: Shipped under ambient temperature as non-hazardous chemical or refer to Certificate of Analysis
Storage Condition: Dry, dark and -20 oC for 1 year or refer to the Certificate of Analysis.
Shelf Life: ≥12 months if stored properly.
Stock Solution Storage: 0 - 4 oC for 1 month or refer to the Certificate of Analysis.
Drug Formulation: To be determined
HS Tariff Code: 382200
How to use
In Vitro:
The enzyme displays high hydrolysis ability for ONPG (100%) and moderate activity for its natural substrate lactose (25.7%). However, the hydrolysis ability of the enzyme towards all other chromogenic nitrophenyl analogues is very weak, indicating that Gal308 is a β-galactosidase with narrow substrate specificity. To investigate the kinetic parameters of recombinant enzyme, the Michaelis-Menten constants (Km), turnover numbers (kcat), and catalytic efficiencies (kcat/Km) of Gal308 for ONPG and lactose are determined. The kcat and Km values are 464.7±7.8 s-1 and 2.7±0.3 mM for ONPG, and 264.2±2.1 s-1 and 7.1±0.8 mM for lactose, respectively. The kcat/Km value of the enzyme for ONPG (172.1 s-1mM-1) is 4.6-fold higher than that for lactose (37.2 s-1mM-1), which clearly demonstrated that the catalytic efficiency of Gal308 for ONPG is much higher than that for lactose.
References:
- Zhang X, et al. Metagenomic approach for the isolation of a thermostable β-galactosidase with high tolerance of galactose and glucose from soil samples of Turpan Basin. BMC Microbiol. 2013 Oct 24;13:237. doi: 10.1186/1471-2180-13-237.
Products are for research use only. Not for human use.
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