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71230 Lysonase™ Bioprocessing Reagent

71230
Purchase on Sigma-Aldrich

Áttekintés

Replacement Information

Products

KatalógusszámCsomagolás Menny./csomag
71230-3 Üvegpalack 0.2 ml
71230-4 Muanyagampulla 1 ml
Description
Overview

Lysonase™ Bioprocessing Reagent is an optimized, ready-to-use blend of rLysozyme™ Solution and Benzonase Nuclease. rLysozyme Solution contains a highly purified and stabilized recombinant lysozyme with specific activity 250 times greater than that of chicken egg white lysozyme. Benzonase Nuclease is a genetically engineered nonspecific endonuclease that degrades all forms of DNA and RNA (single stranded, double stranded, circular, linear), reducing extract viscosity and increasing protein yield. The combined activities of rLysozyme and Benzonase Nuclease significantly increase protein extraction efficiency and facilitate downstream processing of protein extracts. For efficient protein extraction with BugBuster® Protein Extraction Reagent, use 10 µl Lysonase per 1 g cell paste. For efficient protein extraction with PopCulture® Reagent, add 2 µl Lysonase per 1 ml culture. Store at –20°C.

Catalogue Number71230
Brand Family Novagen®
References
Product Information
Quality LevelMQ400
Applications
Biological Information
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Blue Ice Only
Toxicity Standard Handling
Storage -20°C
Do not freeze Ok to freeze
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Katalógusszám GTIN
71230-3 07790788053116
71230-4 04055977271195

Documentation

Lysonase™ Bioprocessing Reagent Certificates of Analysis

TitleLot Number
71230

Brochure

Title
Benzonase®Nuclease
Bulk Product Guide
Protein Purification and Detection Tools

Technical Info

Title
Benzonase®endonuclease for improved primary recovery in an E. coli-based process for Fab production

Citations

Titulus
  • Johannes Mullegger, et al. (2005) Engineering of a thioglycoligase: randomized mutagenesis of the acid-base residue leads to the identification of improved catalysts. Protein Engineering Design and Selection 18, 33-40.
  • Dirk Hoffmeister and Jon S. Thorson. (2004) Mechanistic implications of Escherichia coli galactokinase structure-based engineering. ChemBioChem 5, 989-992.
  • Dirk Hoffmeister, et al. (2003) Creation of the first anomeric D/L-sugar kinase by means of directed evolution. Procedings of the National Academy of Science 100, 13184-13189.
  • User Protocols

    Title
    TB361 Lysonase™ Bioprocessing Reagent