Analytical Data
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Gene name
MTR_4g091000
- Application
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Alternative Names
(Putative LysM domain-containing protein)
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Species
Medicago truncatula
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
G7JRT4
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Expression Region
29-81aa
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Molecular Weight
13.3 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
The research background of MTR_4g091000, a recombinant protein, is rooted in its potential functional significance within various biological processes. MTR_4g091000 is a gene identified in the model organism *Methylobacterium extorquens*, which plays a crucial role in the methanol metabolism pathway. This organism is notable for its ability to utilize one-carbon compounds, making it a subject of interest for biotechnological applications, such as bioremediation and biofuel production. Understanding the structure and function of recombinant MTR_4g091000 can provide insights into its enzymatic activities and regulatory mechanisms. The study of this protein may reveal vital information regarding cellular responses to environmental stressors and metabolic adaptations. Furthermore, MTR_4g091000 may have implications in synthetic biology, where it could be harnessed for engineering microbial strains with enhanced capabilities in converting methanol into valuable metabolic products. As the demand for sustainable energy sources and environmental solutions grows, unraveling the biochemical properties of proteins like MTR_4g091000 becomes increasingly important. Consequently, research focusing on its expression, purification, and functional characterization not only contributes to the foundational knowledge of microbial metabolism but also paves the way for innovative applications in environmental and industrial biotechnology.
