Analytical Data
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Gene name
lytM
- Application
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Alternative Names
Autolysin LytM
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Species
Staphylococcus aureus
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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
O33599
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Expression Region
26-316aa
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Molecular Weight
35.9 kDa
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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
LytM protein, a member of the large family of metalloproteases, plays a critical role in various biological processes, including bacterial cell wall degradation and regulation of protein turnover. The significance of LytM proteins has garnered attention in the context of bacterial pathogenesis, where they facilitate the breakdown of peptidoglycan, thereby enabling bacteria to alter their cell shape or escape immune responses. This capability makes LytM an attractive target for the development of novel antimicrobial strategies aimed at combating antibiotic-resistant infections. Researchers have been investigating the structure-function relationship of LytM proteins to elucidate their enzymatic mechanisms and identify potential inhibitors. Advances in protein engineering techniques and high-throughput screening methods have further accelerated the exploration of LytM, leading to promising findings that may pave the way for new therapeutic interventions. Understanding the role of LytM in various organisms not only enhances our knowledge of microbial physiology but also provides insights into evolutionary adaptations that have allowed some bacteria to thrive in hostile environments. Consequently, the study of LytM proteins carries significant implications for both basic science and clinical applications in the fight against infectious diseases.
