Analytical Data
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Gene name
murG
- Application
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Alternative Names
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
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Species
Bacillus subtilis
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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
P37585
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Expression Region
1-363aa
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Molecular Weight
43.9 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
MurG is a crucial enzyme involved in the bacterial cell wall biosynthesis pathway, specifically in the synthesis of peptidoglycan, which provides structural integrity to bacterial cells. The enzyme catalyzes the transfer of the MurNAc-GlcNAc moiety to the growing peptidoglycan chain, making it a key target for understanding bacterial growth and survival. Research on murG recombinant proteins has gained prominence due to the rise of antibiotic-resistant bacterial strains, emphasizing the need for new therapeutic strategies. By producing murG in a recombinant system, researchers can obtain large quantities of the protein for detailed structural and functional analyses. This research not only elucidates the enzyme's role in cell wall synthesis but also aids in the identification of potential inhibitors that could serve as novel antibacterial agents. The study of murG and its recombinant forms is thus significant for both fundamental microbiology and the development of innovative antimicrobial therapies, offering insights that could lead to more effective treatments against resistant bacterial infections. This growing body of work underscores the importance of understanding bacterial physiology and the potential for exploiting specific enzymatic pathways in drug discovery efforts.
