Analytical Data
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Gene name
cwlM
- Application
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Alternative Names
Autolysin;Cell wall hydrolase
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Species
Bacillus licheniformis
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P37134
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Expression Region
1-253aa
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Molecular Weight
43.6 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
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Protein Description
CwlM, a member of the Cwl family of proteins, has garnered significant attention in the field of microbiology and biotechnology due to its potential roles in bacterial cell wall metabolism and its implications for antibiotic resistance. This protein is primarily derived from the bacterium *Bacillus subtilis*, which serves as a model organism for studying cellular processes. The CwlM protein is involved in the hydrolysis of beta-glucan, a critical component of the bacterial cell wall, which suggests its potential utility in the development of novel antibacterial agents or biocontrol methods. The understanding of CwlM's structural and functional characteristics is vital, as it opens up possibilities for engineering recombinant forms of the protein that could enhance its activity or target specificity. Furthermore, the study of CwlM contributes to a broader understanding of how bacterial pathogens can remodel their cell wall to adapt to environmental stresses and evade immune responses, making it an important topic in the context of global health challenges posed by antibiotic-resistant infections. Ongoing research into the mechanistic pathways involving CwlM may facilitate the design of innovative strategies in pathogen management, highlighting its relevance in both academic and applied microbiological research.
