Analytical Data
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基因名
RFP
- Application
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别名
Red fluorescent protein drFP583; drFP583; DsRed
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种属
Others
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表达系统
E. coli
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标签
C-6*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9U6Y8
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表达区间
M1-L225
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氨基酸序列
MRSSKNVIKEFMRFKVRMEGTVNGHEFEIEGEGEGRPYEGHNTVKLKVTKGGPLPFAWDILSPQFQYGSKVYVKHPADIPDYKKLSFPEGFKWERVMNFEDGGVVTVTQDSSLQDGCFIYKVKFIGVNFPSDGPVMQKKTMGWEASTERLYPRDGVLKGEIHKALKLKDGGHYLVEFKSIYMAKKPVQLPGYYYVDSKLDITSHNEDYTIVEQYERTEGRHHLFL
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蛋白长度
Full Length
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分子量
36 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.
