-Galactosidase Enzyme from E. coli

-Galactosidase Enzyme from E. coli Catalog Number: B2016616 (2 mg)

-Galactosidase Enzyme from E. coli is offered as a biotechnology-grade powder in a defined 2mg fill (Catalog B2016616) with storage at 20C. The supplier specifies a native E. coli -galactosidase preparation positioned as a molecular tool for various biochemical applications, with concise documentation fields for amount, format, storage and keyword identity. For labs that routinely work with carbohydrate processing, reporter systems, or -galactoside substrates, this clear specification set supports straightforward SOP inclusion and inventory traceability.

-Galactosidase is a benchmark hydrolase that cleaves -galactosidic linkages and is widely used to generate qualitative readouts in method development, instrument checks, and training exercises. A powder format enables precise mass-based dosing and flexible buffer selection tailored to the matrix at hand. Because no working concentration is prescribed on this listing, good practice is to establish conditions empirically: run small pilots that titrate enzyme amount, buffer components and pH, incubation time and temperature; document lot identifiers and time-at-temperature so performance is reproducible across runs and operators. This approach also helps define activity windows that minimize background and ensure consistent behavior across plates, membranes or other bench setups.

Typical research scenarios include creating hydrolysis controls for -galcontaining substrates, assembling reporter workflows where -gal activity serves as a convenient signal, and drafting platform-qualification checks that require a well-characterized enzyme. The biotechnology-grade notesolutions prepared using TypeI ultrapure water and fine filtrationaligns with expectations for low background during optimization. Within research-only boundaries, this native E. coli -galactosidase provides a dependable, clearly specified component for laboratories standardizing -galactoside hydrolysis and reporter-enzyme workflows.

Why researchers choose this product:

• Defined 2mg fill in powder format for accurate dosing and flexible buffer selection
• Supplier notes native E. coli -galactosidase suitable as a molecular tool for diverse workflows
• Specified storage at 20C supports routine cold-chain handling
• Concise documentation fields (amount, supplied-as, storage, keywords) streamline SOP/LIMS mapping
• Biotechnology-grade note (Type I water; 0.22m filtration for solutions) aligns with low-background expectations

This product is for Research Use Only (RUO). It is not intended for diagnostic or therapeutic use.

References

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• 2: Nepal MR, Kang Y, Kang MJ, Nam DH, Jeong TC. A -galactosidase-expressing E. coli culture as an alternative test to identify skin sensitizers and non-sensitizers J Toxicol Environ Health A. 2018;81(9):288-301.
• 3: Flores SS, Clop PD, Barra JL, Argaraa CE, Perillo MA, Nolan V, Snchez JM. His-tag -galactosidase supramolecular performance Biophys Chem. 2022 Feb;281:106739.
• 4: Berhanu S, Ueda T, Alix JH. The Escherichia coli DnaK chaperone stimulates the -complementation of -galactosidase J Basic Microbiol. 2022 Jun;62(6):669-688.
• 5: Hall BG. The EBG system of E. coli: origin and evolution of a novel beta-galactosidase for the metabolism of lactose Genetica. 2003 Jul;118(2-3):143-56.
• 6: Nepal MR, Kim GH, Cha DH, Jeong TC. Assessment of skin sensitizing potential of metals with -galactosidase-expressing E. coli culture system J Toxicol Environ Health A. 2019;82(15):879-889.
• 7: Jacobson RH, Zhang XJ, DuBose RF, Matthews BW. Three-dimensional structure of beta-galactosidase from E. coli Nature. 1994 Jun 30;369(6483):761-6.
• 8: Herwig E, Marchetti-Deschmann M, Wenz C, Rfer A, Allmaier G. Immunoprecipitation combined with microchip capillary gel electrophoresis: Detection and quantification of -galactosidase from crude E. coli cell lysate Biotechnol J. 2011 Apr;6(4):420-7.
• 9: Dada L, Colomer JP, Manzano VE, Varela O. Synthesis of thiodisaccharides related to 4-thiolactose. Specific structural modifications increase the inhibitory activity against E. coli -galactosidase Org Biomol Chem. 2023 Mar 8;21(10):2188-2203.
• 10: Brockhaus M, Dettinger HM, Kurz G, Lehmann J, Wallenfels K. Participation of HO-2 in the cleavage of beta-D-galactosides by the beta-D-galactosidase from E. coli Carbohydr Res. 1979 Mar;69:264-8. pubmed.ncbi.nlm.nih.gov