关键信息
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基因名
DDTL
- 应用
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别名
(D-dopachrome tautomerase-like protein)
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种属
Human
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
A6NHG4
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表达区间
1-134aa
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分子量
21.6 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.
质检流程
相关产品
背景信息
DDTL (Double-Domain Toxin-Like) recombinant proteins have garnered significant attention in the field of biochemistry and molecular biology due to their unique structural and functional properties. Originally inspired by natural toxin proteins, which exhibit potent biological activities, researchers have sought to harness the potential of DDTL proteins for various applications, including therapeutic development and biotechnological innovations. The study of DDTL proteins is driven by their dual-domain architecture, which allows for enhanced specificity and functionality by combining distinct biochemical properties from each domain. This has opened avenues for creating novel biosensors, targeted drug delivery systems, and therapeutic agents with reduced side effects. Additionally, DDTLs' capacity for engineering and modification makes them valuable candidates in the ongoing quest to design more effective and safe biomolecules. Research has focused on elucidating the mechanisms of action of these proteins, optimizing their production in recombinant systems, and exploring their interactions with biological targets. As a result, DDTL proteins represent a promising frontier in the development of advanced materials and therapeutics, with the potential to address various challenges in medicine and biotechnology.
