Analytical Data
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Gene name
RFP
- Application
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Alternative Names
Red fluorescent protein drFP583; drFP583; DsRed
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Species
Others
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Source
E. coli
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Tag
C-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9U6Y8
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Expression Region
M1-L225
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AA Sequence
MRSSKNVIKEFMRFKVRMEGTVNGHEFEIEGEGEGRPYEGHNTVKLKVTKGGPLPFAWDILSPQFQYGSKVYVKHPADIPDYKKLSFPEGFKWERVMNFEDGGVVTVTQDSSLQDGCFIYKVKFIGVNFPSDGPVMQKKTMGWEASTERLYPRDGVLKGEIHKALKLKDGGHYLVEFKSIYMAKKPVQLPGYYYVDSKLDITSHNEDYTIVEQYERTEGRHHLFL
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Protein Length
Full Length
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Molecular Weight
36 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
Related Products
Protein Description
Research on recombinant fibronectin type III domain-containing protein (RFP) has gained significant attention in recent years due to its potential applications in various fields, including biotechnology, medicine, and tissue engineering. RFPs are engineered proteins derived from parental structures that possess unique binding and biological properties, making them ideal candidates for therapeutic interventions and diagnostic tools. The ability to produce RFPs in large quantities using recombinant DNA technology allows for comprehensive studies on their functional characteristics. Recent advancements in protein engineering, such as directed mutagenesis and high-throughput screening techniques, enable researchers to optimize the properties of RFPs for specific applications. Moreover, the study of RFPs is not only crucial for understanding fundamental biological processes but also holds promise for the development of innovative treatments for diseases, including cancer and autoimmune disorders. The integration of RFPs in drug delivery systems and nanoparticle formulations has further enhanced their relevance in modern medicine. Consequently, ongoing research efforts aim to elucidate the mechanisms through which RFPs operate and to harness their capabilities for translational applications, addressing unmet medical needs through improved therapeutic strategies.
