Analytical Data
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Gene name
yccG
- Application
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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
P70954
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Expression Region
1-318aa
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Molecular Weight
36.6 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
Related Products
Protein Description
YccG is a protein of interest due to its potential roles in various biological processes, particularly in bacterial physiology and stress response mechanisms. Originally identified in Escherichia coli, YccG belongs to a family of proteins that are hypothesized to be involved in the regulation of gene expression and cellular adaptation to environmental changes. Research has suggested that YccG may function as a regulatory factor linked to the synthesis of secondary metabolites or in response to oxidative stress, suggesting its role in maintaining cellular homeostasis. The recombinant expression of YccG provides a unique opportunity to study its structure-function relationship and understand its biochemical properties. By utilizing techniques such as cloning, expression in heterologous systems, and purification, researchers aim to characterize YccG at the molecular level. This research is crucial for elucidating the protein's function and its involvement in bacterial survival strategies. Moreover, understanding YccG could provide insights into new antimicrobial targets, given the increasing prevalence of antibiotic resistance. The continued investigation of YccG's properties and functions promises to enhance our knowledge of bacterial biology and contribute to the development of innovative therapeutic strategies.
