Lysozyme from chicken egg, ca. 20000 U/mg
Advantages at a glance
- Activity: min. 20,000 U/mg (pH6.25)
- Appearance: white freeze-dried powder, albumin-free
- MW: approx. 14,400 g/mol
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Product information "Lysozyme from chicken egg, ca. 20000 U/mg"
The enzyme Lysozyme (Muramidase) affects the cell walls of bacteria. Thereby the extraction efficiency of proteins or nucleic acids is significantly improved. Genaxxon Lysozyme from chicken egg is available as lyophilized powder.
Lysozyme preferentially hydrolyses the β-1,4-glycosidic binding between N-Acetyl muraminic acid and N-Acetyl glucosamine, a component of the proteoglycan-cell wall of certain microorganisms. The enzyme is present in many organisms. In molecular biology, the enzyme from chicken white egg is used to lyse E. coli for the isolation of plasmid-DNA. The lysis of E.coli is improved by the combined addition of both lysozyme and and a nuclease such as DNase I (M3028) >. The working concentration is 200-300 μg/µL. To increase the plasmid yield (approx. 5-10%), lysozyme may be added. Another application is the lysis of bacteria for the preparation of bacterial RNA. In this case the working concentration is 40μg/mL (stock solution 50mg/mL).
Lysozyme from chicken egg is most effective for the lysis of gram-positive bacteria. Besides this, it facilitates the lysis of gram-negative bacteria such as Salmonella and Shigella.
- Lyophilized, white powder
- Enzyme for lysis of bacterial cell walls
- Improvement of protein purification from inclusion bodies
- Activity: min. 20.000 U/mg (pH: 6.25)
Lysozyme will be inhibited by surfactants like SDS (M3292) > or alcohols and fatty acids, Imidazole (M6033) > and Indol-derivatives.
Stability: The lyophilized powder of lysozyme is stable for many years at +2°C to +8°C. In solution, the stability at pH values from 4 to 5 at +2°C to +8°C is several weeks and at room temperature several days. pH-optimum is at 9.2, the isoelectric point at 11.0.
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