Recombinant T4 Lysozyme (1 mg/mL)
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Recombinant T4 Lysozyme (1 mg/mL)

Cat.No: IVDRM-0199 Datasheet

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Product Name Recombinant T4 Lysozyme (1 mg/mL)
Catalog No. IVDRM-0199
Description T4 Lysozyme is a recombinant muramidase derived from T4 bacteriophage. It disrupts bacterial cell walls by hydrolyzing the beta-1,4 glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine in the peptidoglycan of prokaryotic cells, including Gram-negative bacteria and some Gram-positive bacteria. It can be used to extract soluble proteins, membrane proteins, DNA, RNA, or metabolites. Expressed in a recombinant E. coli strain and free of animal-derived components, this enzyme exhibits activity several hundred times higher than lysozyme extracted from hen egg white, so far less enzyme is needed and lysis time is greatly shortened. Each milligram of the product can lyse at least 30 g of cells. It can be used directly for rapid bacterial lysis, and the resulting lysate can be used immediately and is compatible with affinity resins. The product is also compatible with a wide range of downstream applications, including SDS-PAGE, Western blot, activity assays, immunoprecipitation, and downstream purification.
Intended Use For bacterial cell wall disruption and extraction of soluble proteins, membrane proteins, DNA, RNA, or metabolites from Gram-negative bacteria and some Gram-positive bacteria.
Principle / Technology T4 Lysozyme is a muramidase that hydrolyzes the beta-1,4 glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine in bacterial peptidoglycan, thereby disrupting the cell wall. It is produced by a recombinant E. coli strain and is free of animal-derived components.
Sample Type Prokaryotic cells, including Gram-negative bacteria and some Gram-positive bacteria.
Performance Range / Specifications Protein purity: >=95%
Activity: several hundred times higher than hen egg white lysozyme
Lytic capacity: each mg of product lyses at least 30 g of cells
No detectable nicking enzyme or RNase residues (verified across 3 batches by agarose gel electrophoresis with 1 µg enzyme per assay)
Specificity Hydrolyzes the beta-1,4 bonds between N-acetylmuramic acid and N-acetylglucosamine in the peptidoglycan of prokaryotic cells (Gram-negative bacteria and some Gram-positive bacteria).
Reaction Conditions / Protocol Typical lysis protocol: resuspend a 1 g bacterial cell pellet in 30 mL of 50 mM Tris-HCl, 0.5 mM EDTA, pH 7.5 buffer; add 0.1-2 µg of enzyme per mL of cell suspension; lyse at room temperature for 5 minutes with gentle inversion (or standing). Collect soluble proteins by centrifugation at 12,000 g for 30 minutes at 4°C and analyze by SDS-PAGE.
Components / Formulation Recombinant T4 Lysozyme supplied as a solution at 1 mg/mL.
Storage Conditions Store at -25 to -15°C.
Shelf Life 2 years when stored at -25 to -15°C.
Package Specifications 200 µg; 1 mg
Product Form Solution
Quality Control Protein purity >=95%. No nicking enzyme or RNase residues detected: enzyme was incubated with nucleic acid substrates and analyzed by agarose gel electrophoresis, and no nicking enzyme (1 µg) or RNase (1 µg) residues were detected in any of the 3 batches tested.
Purity Protein purity >=95%
Concentration 1 mg/mL
Activity / Unit Definition Each mg of product lyses at least 30 g of cells; activity is several hundred times higher than lysozyme extracted from hen egg white.
Source / Origin Derived from T4 bacteriophage; expressed in a recombinant E. coli strain; free of animal-derived components.
Expiration Date / Stability Valid for 2 years when stored at -25 to -15°C.
Compatibility Lysates can be used directly and are compatible with affinity resins. Compatible with downstream applications such as SDS-PAGE, Western blot, activity assays, immunoprecipitation, and downstream purification.
Recommended Buffer System 50 mM Tris-HCl, 0.5 mM EDTA, pH 7.5
Batch-to-Batch Consistency No nicking enzyme or RNase residues were detected in any of the 3 batches tested.

For research use only, not for clinical use.

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