Analytical Data
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Gene name
DERF6
- Application
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Alternative Names
(Allergen Der f VI)(DF5)(allergen Der f 6)
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Species
Dermatophagoides farinae
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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
P49276
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Expression Region
50-279aa
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Molecular Weight
32.5 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
DERF6 is a recently identified member of the DERF family of proteins, which are characterized by the presence of DEAH box motifs and are implicated in various biological processes, including RNA metabolism and cellular stress responses. Its potential role in regulating gene expression and influence on cell proliferation makes it an intriguing target for study. Research has shown that DERF6 is expressed in multiple tissues, suggesting its involvement in diverse physiological processes. Previous studies have indicated that DERF family proteins may play a significant role in modulating developmental pathways and stress responses in plants, yet the specific functional mechanisms of DERF6 remain largely uncharacterized. This gap in knowledge highlights the necessity for detailed investigations into the structure-function relationship of DERF6, its interaction with other cellular proteins, and its influence on gene regulatory networks. Furthermore, understanding the signal transduction pathways involving DERF6 could provide insights into its potential applications in biotechnology, particularly in improving stress tolerance in crops. Recent advances in recombinant protein technology enable the production and purification of DERF6 for functional assays, facilitating a deeper exploration of its biological role and mechanisms of action in cellular contexts. Overall, the study of DERF6 is poised to contribute significantly to our understanding of plant biology and the molecular underpinnings of stress responses.
