Analytical Data
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基因名
TTN
- Application
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别名
Connectin Rhabdomyosarcoma antigen MU-RMS-40.14
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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
Q8WZ42
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表达区间
14257-14543aa
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分子量
36.9 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
TTN, or Titin, is a colossal protein that plays a crucial role in the structure and function of striated muscle tissues, being the largest known protein in the human body. Its intricate function is primarily linked to muscle contraction and elasticity, serving as a molecular spring that helps maintain the integrity of the muscle sarcomere during stretching and contraction. Research into TTN has gained momentum due to its involvement in myopathies and cardiomyopathies, with numerous mutations associated with these conditions. The complexity of TTN's structure, comprising over 38,000 amino acids, presents significant challenges for researchers, particularly in deciphering its diverse functional domains and their roles in muscle mechanics. Advances in recombinant protein technology have enabled the production of smaller fragments of TTN, allowing for a more detailed study of its functional properties. Furthermore, elucidating the molecular mechanisms behind TTN-related disorders can pave the way for potential therapeutic strategies, including gene therapy and precision medicine approaches. As the field continues to evolve, the investigation of TTN and its related proteins remains essential for developing a comprehensive understanding of muscle biology and pathology.












