Analytical Data
-
Gene name
MTR_4g091020
- Application
-
Alternative Names
(Putative LysM domain-containing protein)
-
Species
Medicago truncatula
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
G7JRT6
-
Expression Region
26-87aa
-
Molecular Weight
19.7 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
The study of the MTR_4g091020 recombinant protein is rooted in the ongoing exploration of microbial physiology and metabolic pathways, particularly in the context of environmental adaptations. MTR_4g091020, encoded by a gene in the *Methylophilus methylotrophus* genome, is hypothesized to play a crucial role in the organism’s ability to utilize methanol as a carbon source. Understanding this protein's structure and function can provide insights into how methylotrophic bacteria contribute to carbon cycling and potentially enhance biotechnological applications, such as biofuel production and bioremediation. Given the increasing interest in sustainable practices and the need for innovative solutions to environmental challenges, examining the MTR_4g091020 protein could reveal novel enzymatic functions or regulatory mechanisms that could be harnessed for industrial purposes. Recent advancements in recombinant DNA technology allow for the efficient production and characterization of this protein, facilitating its functional analysis. Investigations into MTR_4g091020 not only aim to delineate its biological role but also seek to assess its potential as a biocatalyst in synthetic biology applications. Therefore, the research on this protein could bridge fundamental microbial research and practical biotechnological advances, providing a deeper understanding of methylotrophy and its implications for ecological and industrial processes.
