Analytical Data
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Gene name
yciM
- Application
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Species
Escherichia coli
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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
P0AB58
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Expression Region
17-389aa
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Molecular Weight
46.9 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
YciM is a protein originally identified in Escherichia coli, and it has gained attention due to its potential roles in various biological processes. Research into YciM has revealed its involvement in cellular functions such as stress response, biofilm formation, and gene regulation. The protein belongs to a family of conserved proteins, suggesting that it may play a critical role in the bacterial life cycle. However, its exact biochemical functions and mechanisms remain largely uncharacterized, creating a gap in our understanding of its physiological significance. Recent studies have focused on the recombinant expression of YciM to elucidate its structure and function, employing techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. By producing YciM as a recombinant protein, researchers aim to explore its interactions with other biomolecules and its impact on bacterial behavior under various environmental conditions. This research is not only pivotal for understanding bacterial physiology but may also have implications for developing antibacterial strategies targeting YciM-related pathways. Thus, the investigation of YciM and its recombinant counterpart presents a promising avenue for advancing our comprehension of microbial biology and addressing related health challenges.
