Analytical Data
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基因名
TTN
- Application
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别名
TTN；Titin
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种属
Human
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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
Q8WZ42
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表达区间
5398-5604aa
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氨基酸序列
VFKCSVIGIPTPEVKWYKEYMCIEPDNIKYVISEEKGSHTLKIRNVCLSDSATYRCRAVNCVGEAICRGFLTMGDSEIFAVIAKKSKVTLSSLMEELVLKSNYTDSFFEFQVVEGPPRFIKGISDCYAPIGTAAYFQCLVRGSPRPTVYWYKDGKLVQGRRFTVEESGTGFHNLFITSLVKSDEGEYRCVATNKSGMAESFAALTLT
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分子量
26.5kDa
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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 (titin) is one of the largest known proteins and plays a crucial role in the structure and function of striated muscle fibers, contributing to their elasticity and stability. It serves as a molecular scaffold, connecting myofilaments and maintaining sarcomere integrity during muscle contraction. Research on TTN recombinant proteins has become increasingly relevant due to their importance in understanding muscle physiology and pathophysiology. Mutations in the TTN gene are linked to various muscular diseases, including dilated cardiomyopathy and skeletal myopathies, making it essential to investigate the functional implications of these variants. By producing recombinant TTN proteins, researchers aim to explore their biochemical properties, interaction dynamics, and the effects of specific mutations on muscle function. This line of inquiry not only enhances our understanding of TTN’s role in muscle mechanics but also aids in the development of therapeutic strategies for TTN-related diseases. Additionally, recombinant TTN proteins provide a valuable tool for investigating the mechanisms underlying muscle contraction and the potential for regenerative therapies, positioning TTN research at the forefront of both basic and applied muscle biology studies.
