Analytical Data
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Gene name
rodA
- Application
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Alternative Names
rodA；CLECSF8；MCL；C-type lectin domain family 4 member D
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P41746
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Expression Region
19-159aa
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AA Sequence
LPQHDVNAAGNGVGNKGNANVRFPVPDDITVKQATEKCGDQAQLSCCNKATYAGDVTDIDEGILAGTLKNLIGGGSGTEGLGLFNQCSKLDLQIPVIGIPIQALVNQKCKQNIACCQNSPSDASGSLIGLGLPCIALGSIL
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Molecular Weight
16.3 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
RodA is a crucial protein involved in the maintenance of cell shape and integrity in various bacteria, particularly in rod-shaped bacteria such as Escherichia coli. It plays a significant role in peptidoglycan synthesis, which is essential for cell wall formation and overall cell functionality. Studies have shown that RodA is an important factor in the regulation of cell growth and division, and its activity is closely linked to the bacterial cytoskeleton. Research on RodA has gained momentum due to its potential as a target for new antibiotic development, especially in the context of rising antibiotic resistance. Understanding the structure, function, and regulation of RodA can provide insights into the fundamental processes of bacterial morphology and growth, contributing to the design of novel antibacterial strategies. Through techniques like X-ray crystallography and cryo-electron microscopy, researchers aim to elucidate the molecular mechanisms of RodA's involvement in cell wall biosynthesis and assess its interactions with other proteins in the bacterial context. This research not only enhances our comprehension of bacterial physiology but also holds promise for innovative therapeutic approaches in combating bacterial infections.
