Analytical Data
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基因名
TTC9B
- Application
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别名
TTC9B; Tetratricopeptide repeat Protein 9B; TPR repeat Protein 9B
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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
Q8N6N2
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表达区间
1-239 aa
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氨基酸序列
MQRGALSPVL MLSAAPEPPP RPPPALSPPG SGPGSGSRHG SARPGPTPEP SGSLGAALDS SLRAAVAFKA EGQRCYREKK FREAIGKYHR ALLQLKAAQG ARPSGLPAPA PGPTSSPGPA RLSEEQRRLV ESTEVECYDS LTACLLQSEL VNYERVREYC LKVLEKQQGN FKATYRAGIA FYHLGDYARA LRYLQEARSR EPTDTNVLRY IQLTQLKMNR CSLQREDSGA GSQTRDVIG
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分子量
25.9 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
TTC9B (Tetratricopeptide Repeat Domain 9B) is a protein that has garnered attention due to its potential involvement in various biological processes and diseases. Emerging evidence suggests that TTC9B plays a critical role in cellular mechanisms, including protein-protein interactions and intracellular signaling pathways. Research has indicated that TTC9B may be implicated in neurodegenerative disorders and certain types of cancers, highlighting its significance in health and disease. The study of TTC9B, particularly in its recombinant form, allows for a more detailed examination of its functional properties and interactions. Recombinant protein technologies provide a means to produce TTC9B in controlled laboratory settings, allowing researchers to explore its structure and biochemical activities. Understanding the functional dynamics of TTC9B could lead to insights into its role in pathophysiological conditions and potentially uncover new therapeutic targets. Moreover, the engineering of TTC9B for experimental applications could enhance our capability to manipulate cellular pathways and investigate its role in disease mechanisms, making it a promising candidate for future biotechnological applications. Overall, the exploration of TTC9B as a recombinant protein represents a vital area of research with implications for understanding fundamental biological processes and developing novel strategies for disease intervention.
