Analytical Data
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Gene name
rpmD
- Application
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Alternative Names
rpmD；Large ribosomal subunit Protein uL30
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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
P0AG51
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Expression Region
1-59aa
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AA Sequence
MAKTIKITQTRSAIGRLPKHKATLLGLGLRRIGHTVEREDTPAIRGMINAVSFMVKVEE
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Molecular Weight
33.5kDa
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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
The study of RPMD (Regulator of Phosphate Metabolism and Development) recombinant proteins has gained increasing attention due to their critical role in various biological processes, particularly in plant development and response mechanisms to environmental stresses. As a member of the larger family of regulatory proteins, RPMD is involved in phosphate signaling pathways, which are essential for plant growth and nutrient uptake. Understanding the structure and function of RPMD can provide insights into how plants adapt to phosphate availability, which is a significant factor affecting agricultural productivity. Recent advances in protein engineering and recombinant DNA technology have enabled researchers to produce RPMD proteins in heterologous systems, allowing for detailed biochemical characterization and functional studies. These studies have revealed the potential of RPMD as a target for genetic manipulation to enhance phosphate efficiency in crops, thus contributing to sustainable agriculture. Moreover, the exploration of RPMD's interactions with other signaling molecules can further elucidate the complex regulatory networks governing plant responses to nutrient stress. Consequently, research on RPMD recombinant proteins not only enhances our understanding of plant physiology but also opens avenues for developing innovative strategies to improve crop resilience and yield in the face of nutrient challenges.
