Analytical Data
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Gene name
lytM
- Application
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Alternative Names
lytM；Glycyl-glycine endopeptidase LytM
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Species
E.coli
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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
O33599
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Expression Region
26-316aa
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AA Sequence
AETTNTQQAHTQMSTQSQDVSYGTYYTIDSNGDYHHTPDGNWNQAMFDNKEYSYTFVDAQGHTHYFYNCYPKNANANGSGQTYVNPATAGDNNDYTASQSQQHINQYGYQSNVGPDASYYSHSNNNQAYNSHDGNGKVNYPNGTSNQNGGSASKATASGHAKDASWLTSRKQLQPYGQYHGGGAHYGVDYAMPENSPVYSLTDGTVVQAGWSNYGGGNQVTIKEANSNNYQWYMHNNRLTVSAGDKVKAGDQIAYSGSTGNSTAPHVHFQRMSGGIGNQYAVDPTSYLQSR
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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 (Lysin Motif) proteins belong to a family of peptidoglycan hydrolases, which are essential for bacterial cell wall remodeling and maintenance. They play a critical role in processes such as cell division, differentiation, and response to environmental stress. Recent studies have shown that LytM proteins are involved in various physiological processes across different bacterial species, including pathogenesis in some pathogens, making them potential targets for antimicrobial therapy. The unique structural features of LytM proteins, particularly their catalytic domain, offer insights into their enzymatic mechanisms and substrate specificity. Furthermore, recombinant LytM proteins have been increasingly utilized in biochemical studies to investigate their function and interactions with other cellular components. Understanding the structure-function relationship of LytM proteins can provide significant implications for developing novel antibacterial agents by either inhibiting their function or utilizing them in targeted delivery systems. Overall, the ongoing research into LytM recombinant proteins aims to unravel their biological significance and therapeutic potential in combating bacterial infections.
