Analytical Data
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Gene name
LZM
- 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
Bovine
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04421
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Expression Region
Gly18~Leu147
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Molecular Weight
18kDa
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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
LZM (lysozyme) recombinant proteins have garnered significant attention in biomedical research due to their enzymatic properties and potential therapeutic applications. Lysozyme, an enzyme found in various biological fluids, functions by hydrolyzing the glycosidic bonds in bacterial cell walls, thereby exhibiting antimicrobial activity. The advent of recombinant DNA technology has facilitated the production of LZM in various host systems, including bacteria, yeast, and cell cultures, ensuring high yields and consistent quality. Research has primarily focused on enhancing the stability and activity of lysozyme variants, tailoring them for specific applications such as food preservation, pharmaceutical formulations, and as an adjuvant in vaccines. Furthermore, LZM’s role in innate immunity has inspired investigations into its potential as an immunomodulator, opening avenues for therapeutic interventions in inflammatory conditions and infections. The ability to produce LZM in a sustainable and efficient manner through recombinant methods not only addresses the limitations of natural sourcing but also allows for the exploration of engineered variants with improved properties. As such, the study of LZM recombinant proteins stands at the intersection of enzyme technology, microbiology, and therapeutic innovation, highlighting their importance in both fundamental research and practical applications in health and medicine.
