Analytical Data
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Gene name
LZM
- Application
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Alternative Names
LZM；LZM；Lysozyme C
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P61626
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Expression Region
19-148aa
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AA Sequence
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
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Molecular Weight
30.7kDa
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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
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Protein Description
LZM, or Lysozyme M, is a significant protein that plays a crucial role in the innate immune system by providing antimicrobial activity. It is primarily found in various body fluids, including saliva, tears, and milk, where it contributes to the first line of defense against pathogens. Research on LZM recombinant protein has gained momentum due to its potential applications in therapeutic and diagnostic fields. The ability to produce LZM through recombinant DNA technology allows for large-scale production and purification, making it a valuable tool for studying its biological functions and mechanisms. Additionally, LZM holds promise in biotechnology and pharmaceuticals, as its antibacterial properties can be harnessed to develop new antimicrobial agents, food preservatives, or components in wound healing therapies. Furthermore, the structural analysis of LZM provides insights into its enzymatic mechanism and stability, which are essential for designing effective variants with enhanced potency. As scientists explore its full potential, recombinant LZM represents a fascinating intersection of immunology, microbiology, and biotechnology, paving the way for innovative solutions in health and disease management.
