Analytical Data
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Gene name
dgcQ
- Application
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Alternative Names
Cellulose synthesis regulatory protein
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Species
Escherichia coli
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P76330
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Expression Region
381-564aa
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Molecular Weight
47.5 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
Recombinant DgcQ protein is of significant interest in microbial biotechnology due to its role as a diguanylate cyclase, an enzyme that synthesizes cyclic di-GMP, a critical second messenger involved in various cellular processes. DgcQ, derived from certain bacteria, is known to regulate biofilm formation, motility, and virulence, making it a key player in bacterial adaptation to environmental changes. Understanding the structural and functional properties of DgcQ can provide insights into the mechanisms of cyclic di-GMP signaling pathways, which are crucial for bacterial physiology. With the rise of antibiotic resistance, exploring DgcQ and its mechanisms can also lead to novel therapeutic strategies aimed at disrupting biofilm formation in pathogenic bacteria. Furthermore, recombinant protein technology allows for the production of DgcQ in host organisms, facilitating detailed biochemical analysis and potential applications in synthetic biology. As researchers investigate its interaction with other proteins and cellular components, the comprehensive study of DgcQ could reveal new targets for antimicrobial drug development and enhance our knowledge of bacterial communication and behavior.
