|Related Categories||Chromogenic, Galactoside, Gene Reporter Substrates, Glycobiology, Inhibitors and Substrates,|
|grade||for molecular biology|
ONPG (2-Nitrophenyl β-D-galactopyranoside) is a colorimetric substrate for β-galactosidase.
1 g in poly tube
250 mg in poly bottle
5, 25 g in poly bottle
500 mg in poly tube
β-galactosidase, breaks down lactose into galactose and glucose. β-Galactosidase is not lactose specific and can act on simple galactosides. 2-Nitrophenyl β-D-galactopyranoside hydrolysis results in the release of galactose and a yellow chromogenic compound. The test substrate does not depend on an induced or constitutive permease enzyme to enter the cell, therefore reactions are rapid and occur within a 24-hour period.
A stock solution can be prepared in molecular biology grade water at a concentration of 3 mg/ml. Alternatively, a stock solution of approximately 20.5 mg/ml is prepared in 100 mM sodium phosphate buffer (pH 7.3). Gentle warming may be required to completely dissolve the product.
Customers Also Viewed
≥8.0 units/mg solid
Grade VIII, lyophilized powder, ≥500 units/mg protein
Certificate of Analysis
Certificate of Origin
Sambrook, J., et al. Molecular Cloning: A Laboratory Manual 2nd ed., Plainview, NY , (1989), 16.66
CCAAT/Enhancer Binding Protein β2 Is Involved in Growth Hormone-Regulated Insulin-Like Growth Factor-II Gene Expression in the Liver of Rainbow Trout (Oncorhynchus mykiss) Jay H. Lo and Thomas T. Chen Endocrinology 151, 2128-2139, (2010)
Functional interaction between herpes simplex virus type 2 gD and HVEM transiently dampens local chemokine production after murine mucosal infection. Yoon M, Kopp SJ, Taylor JM, et al. PLoS ONE 6(1), e16122, (2011)
The synergistic effect of Escherichia coli inactivation by sequential disinfection with low level chlorine dioxide followed by free chlorine. Yang W, Yang D, Zhu SY, et al. J. Water Health 10(4), 557-64, (2012)
Overexpression and characterization of a novel transgalactosylic and hydrolytic β-galactosidase from a human isolate Bifidobacterium breve B24. Yi SH, Alli I, Park KH, et al. New Biotechnology 28(6), 806-13, (2011)
Heterologous expression of glycoside hydrolase family 2 and 42 β-galactosidases of lactic acid bacteria in Lactococcus lactis. Schwab C, Sørensen KI, and Gänzle MG Syst. Appl. Microbiol. 33(6), 300-7, (2010)
Beta-galactosidase from Lactobacillus pentosus: purification, characterization and formation of galacto-oligosaccharides. Maischberger T, Leitner E, Nitisinprasert S, et al. Biotechnol. J. 5(8), 838-47, (2010)
Activity modulation and reusability of beta-D-galactosidase confined in sol-gel derived porous silicate glass. Crescimbeni MC, Nolan V, Clop PD, et al. Colloids Surf. B Biointerfaces 76(2), 387-96, (2010)
A new beta-galactosidase with a low temperature optimum isolated from the Antarctic Arthrobacter sp. 20B: gene cloning, purification and characterization. Białkowska AM, Cieśliński H, Nowakowska KM, et al. Arch. Microbiol. 191(11), 825-35, (2009)
Adverse effect of tannery waste leachates in transgenic Drosophila melanogaster: role of ROS in modulation of Hsp70, oxidative stress and apoptosis. Siddique HR, Gupta SC, Mitra K, et al. J. Appl. Toxicol. 28(6), 734-48, (2008)
Characterization of lactose utilization and β-galactosidase in Lactobacillus brevis KB290, the hetero-fermentative lactic acid bacterium. Honda H, Yajima N, and Saito T Curr. Microbiol. 65(6), 679-85, (2012)
Purification and characterization of two phospho-β-galactosidases, LacG1 and LacG2, from Lactobacillus gasseri ATCC33323(T). Honda H, Nagaoka S, Kawai Y, et al. J. Gen. Appl. Microbiol. 58(1), 11-7, (2012)
Ser-796 of β-galactosidase (Escherichia coli) plays a key role in maintaining a balance between the opened and closed conformations of the catalytically important active site loop. Jancewicz LJ, Wheatley RW, Sutendra G, et al. Arch. Biochem. Biophys. 517(2), 111-22, (2012)
Differential expression of ccrA in methicillin-resistant Staphylococcus aureus strains carrying staphylococcal cassette chromosome mec type II and IVa elements. Higgins PG, Rosato AE, Seifert H, et al. Antimicrob. Agents Chemother. 53(10), 4556-8, (2009)
Practical considerations when using temperature to obtain rate constants and activation thermodynamics of enzymes with two catalytic steps: native and N460T-beta-galactosidase (E. coli) as examples. Kappelhoff JC, Liu SY, Dugdale ML, et al. Protein J. 28(2), 96-103, (2009)
Characterization of the bga1-encoded glycoside hydrolase family 35 beta-galactosidase of Hypocrea jecorina with galacto-beta-D-galactanase activity. Gamauf C, Marchetti M, Kallio J, et al. FEBS J. 274(7), 1691-700, (2007)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Need larger quantities for your development, manufacturing or research applications?