Analytical Data
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基因名
CAST
- Application
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别名
CAST；GATSL3；Cytosolic arginine sensor for mTORC1 subunit 1
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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
P20810
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表达区间
1-686aa
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氨基酸序列
MNPTETKAVKTEPEKKSQSTKLSVVHEKKSQEGKPKEHTEPKSLPKQASD TGSNDAHNKKAVSRSAEQQPSEKSTEPKTKPQDMISAGGESVAGITAISG KPGDKKKEKKSLTPAVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEE ENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADS SKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAA PPQEKKRKVEKDTMSDQALEALSASLGTRQAEPELDLRSIKEVDEAKAKE EKLEKCGEDDETIPSEYRLKPATDKDGKPLLPEPEEKPKPRSESELIDEL SEDFDRSECKEKPSKPTEKTEESKAAAPAPVSEAVCRTSMCSIQSAPPEP ATLKGTVPDDAVEALADSLGKKEADPEDGKPVMDKVKEKAKEEDREKLGE KEETIPPDYRLEEVKDKDGKPLLPKESKEQLPPMSEDFLLDALSEDFSGP QNASSLKFEDAKLAAAISEVVSQTPASTTQAGAPPRDTSQSDKDLDDALD KLSDSLGQRQPDPDENKPMEDKVKEKAKAEHRDKLGERDDTIPPEYRHLL DDNGQDKPVKPPTKKSEDSKKPADDQDPIDALSGDLDSCPSTTETSQNTA KDKCKKAASSSKAPKNGGKAKDSAKTTEETSKPKDD
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分子量
102 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
CAST (Calcium/Calmodulin-dependent Serine Protein Kinase) is a crucial player in cellular signal transduction, influencing various physiological processes such as muscle contraction, neurotransmitter release, and gene expression. Its dysfunction has been linked to several pathological conditions, including heart disease, neurodegenerative disorders, and cancer. Given its significant role in these biological pathways, the study of CAST has gained considerable momentum, particularly in the context of developing targeted therapies and understanding the molecular mechanisms underpinning its activity. The recombinant expression of CAST proteins allows for detailed analysis of their structure and function, facilitating the identification of potential drug targets and therapeutic interventions. Investigating the post-translational modifications and interaction networks of CAST through recombinant techniques can elucidate its regulatory mechanisms, providing insights into how alterations in CAST function contribute to disease states. As researchers continue to explore the complexities of CAST and its implications in health and disease, the development of advanced biochemical tools for its manipulation and study remains vital to harness its potential in therapeutic applications. This research not only aims to deepen our understanding of CAST itself but also seeks to highlight its relevance in broader biological contexts.
