Analytical Data
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基因名
TNNT1
- Application
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别名
TNNT1;TNT;Troponin T. slow skeletal muscle
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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
P13805
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表达区间
1-278aa
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氨基酸序列
MSDTEEQEYE EEQPEEEAAE EEEEAPEEPE PVAEPEEERP KPSRPVVPPL IPPKIPEGER VDFDDIHRKR MEKDLLELQT LIDVHFEQRK KEEEELVALK ERIERRRSER AEQQRFRTEK ERERQAKLAE EKMRKEEEEA KKRAEDDAKK KKVLSNMGAH FGGYLVKAEQ KRGKRQTGRE MKVRILSERK KPLDIDYMGE EQLRARSAWL PPSQPSCPAR EKAQELSDWI HQLESEKFDL MAKLKQQKYE INVLYNRISH AQKFRKGAGK GRVGGRWK
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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
TNNT1, or cardiac troponin T, is a crucial component of the troponin complex in cardiac muscle, playing a pivotal role in the regulation of muscle contraction. Mutations in the TNNT1 gene have been linked to various myopathies, particularly familial hypertrophic cardiomyopathy, which underscores the importance of understanding its structure and function. Research on TNNT1 recombinant proteins has gained significance in the field of cardiology and muscle biology, as these proteins provide valuable insights into the molecular mechanisms underlying heart contractility and associated diseases. By producing recombinant TNNT1 in vitro, researchers can analyze its biochemical properties and interactions with other troponin components and myofilament proteins. Additionally, the study of TNNT1 recombinant proteins facilitates the examination of how specific mutations affect troponin function and muscle contraction dynamics. This research is critical for developing targeted therapies and interventions aimed at addressing the pathologies linked to TNNT1 mutations. Furthermore, the recombinant form of TNNT1 serves as a useful tool for high-throughput screening of small molecules that can potentially modulate troponin activity, offering a pathway toward innovative treatments for cardiac disorders. The ongoing investigation into TNNT1 recombinant proteins not only enhances our fundamental understanding of cardiac physiology but also holds promise for advancing therapeutic strategies for a range of cardiovascular conditions.












