Analytical Data
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Gene name
MTR_4g091010
- 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
G7JRT5
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Expression Region
26-85aa
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Molecular Weight
14.1 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 MTR_4g091010 protein, encoded by the gene in the model organism, has garnered significant interest in the field of molecular biology and biotechnology due to its potential roles in various biological processes. This protein is believed to be involved in key metabolic pathways, making it a valuable subject for research aimed at understanding its functions and implications in cellular mechanisms. Initial studies suggest that MTR_4g091010 may play a crucial role in stress response and adaptation in organisms, which could have implications for agricultural practices, especially in enhancing crop resilience to environmental stresses. Furthermore, the exploration of this protein's structure and interactions at the molecular level could provide insights into its function and the broader implications for genetically engineered organisms. Understanding the molecular basis of MTR_4g091010's role could also advance knowledge in areas such as synthetic biology and metabolic engineering, potentially leading to innovative applications in biotechnology. As such, elucidating the functions and regulatory mechanisms of MTR_4g091010 represents a promising avenue for research that may contribute to advancements in both fundamental science and applied agricultural technologies.
