Analytical Data
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Gene name
Lysozyme C/LYZ
- Application
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Alternative Names
LYZ; Renal Amyloidosis; N-Acetylmuramide Glycanhydrolase; Muramidase; 1,4-beta-N-acetylmuramidase C
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P00697
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Expression Region
Lys19~Val148
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Molecular Weight
16kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Lysozyme C (LYZ) is a highly conserved enzyme found in a variety of biological samples, known for its antimicrobial properties. It plays a crucial role in the innate immune system by hydrolyzing the peptidoglycan layer of bacterial cell walls, thus offering a first line of defense against infections. Due to its significant biological functions and potential applications in food preservation, pharmaceuticals, and biotechnology, the production of recombinant LYZ has garnered considerable interest. Advances in molecular cloning and expression systems have enabled the efficient production of LYZ in various host organisms, including bacteria, yeast, and mammalian cells. Research on recombinant LYZ focuses on optimizing expression conditions, improving enzyme stability, and enhancing its antimicrobial activity. Additionally, the structural and functional characterization of LYZ variants can provide insights into enzyme mechanisms and inform the design of more effective antimicrobial agents. The ongoing exploration of recombinant LYZ also highlights its potential as a therapeutic protein in treating microbial infections and as a complementary agent in antibiotic therapy, especially in light of rising antibiotic resistance. Overall, the study of recombinant LYZ represents a promising avenue for developing innovative solutions to combat infectious diseases and improve food safety.
