Analytical Data
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基因名
TTR
- Application
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别名
TTR;PALB;Transthyretin
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种属
MACFA
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q8HXW1
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表达区间
21-147aa
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氨基酸序列
GPTGVDESKCPLMVKVLDAVRGSPAVNVAVNVFKKAADETWAPFASGKTS ESGELHGLTTEEEFVEGIYKVEIDTKSYWKSLGISPFHEHAEVVFTANDS GPRHYTIAALLSPYSYSTTAVVTNPKE
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分子量
15 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
Related Products
Protein Description
Transferrin receptor (TTR) is an important protein involved in the transport of retinol and thyroxine, primarily synthesized in the liver and the choroid plexus of the brain. Recent studies have highlighted its role in various pathological conditions, including neurodegenerative diseases, amyloidosis, and metabolic disorders. TTR itself can misfold and aggregate, leading to the formation of amyloid deposits that can severely compromise organ function. This has spurred research into TTR as a potential therapeutic target, as well as a candidate for recombinant protein studies. Understanding the molecular mechanisms of TTR misfolding and aggregation is essential for developing effective treatments. Recombinant proteins, particularly engineered variants of TTR, are being explored for their ability to stabilize its structure and inhibit amyloid formation. Furthermore, advancements in recombinant DNA technology have enabled the production of various TTR isoforms with specific modifications that could enhance their therapeutic potential. The investigation of TTR recombinant proteins is thus critical, not only for elucidating TTR’s biological functions but also for developing practical applications in drug design and therapeutic interventions for diseases associated with TTR dysfunction.












