Analytical Data
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Gene name
RGF1
- Application
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Alternative Names
RGF1;GPIG4;Ras-GEF domain-containing family member 1B
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Species
Human
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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
Q3E880
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Expression Region
104-116aa
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AA Sequence
DYSNPGHHPPRHN
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Molecular Weight
28.2 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
RGF1, or Regulating Gene Expression Factor 1, is a protein that has garnered increasing interest in molecular biology and genetic research due to its significant role in plant development and stress response mechanisms. Identified in various plant species, RGF1 functions primarily as a growth regulator, influencing root development and cellular differentiation. Its involvement in the regulatory networks that mediate responses to environmental stresses, such as drought and salinity, highlights its potential agricultural applications in enhancing crop resilience. Recent studies have utilized recombinant DNA technology to produce RGF1, allowing for the detailed exploration of its structure, function, and interactions at a molecular level. This research aims not only to elucidate the biochemical pathways associated with RGF1 but also to facilitate the development of genetically modified organisms (GMOs) that can thrive under challenging conditions. The ongoing investigations into RGF1's properties and its synthetic derivatives pave the way for innovative biotechnological approaches, ultimately contributing to sustainable agricultural practices and food security in the face of climate change.











