Analytical Data
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基因名
STYX
- Application
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别名
STYX；Serine/threonine/tyrosine-interacting Protein
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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
Q8WUJ0
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表达区间
1-223aa
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氨基酸序列
MGSSHHHHHH SSGLVPRGSH MGSHMEDVKL EFPSLPQCKE DAEEWTYPMR REMQEILPGL FLGPYSSAMK SKLPVLQKHG ITHIICIRQN IEANFIKPNF QQLFRYLVLD IADNPVENII RFFPMTKEFI DGSLQMGGKV LVHGNAGISR SAAFVIAYIM ETFGMKYRDA FAYVQERRFC INPNAGFVHQ LQEYEAIYLA KLTIQMMSPL QIERSLSVHS GTTGSLKRTH EEEDDFGTMQ VATAQNG
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分子量
28 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
STYX is a member of the phosphatase family, known for its role in dephosphorylating serine and threonine residues. Its significance has emerged in various cellular processes, including signal transduction, cell cycle regulation, and apoptosis. Recent studies suggest that STYX may play a pivotal role in modulating stress responses and neurodegenerative diseases, making it a potential therapeutic target. The reconstitution of STYX protein allows researchers to investigate its biochemical properties and interactions, providing insights into its function within cellular pathways. Moreover, understanding the structure-function relationship of STYX can illuminate its role in pathological conditions, fostering the development of novel interventions. Given the complexity of post-translational modifications and their impact on protein functionality, the study of STYX reconstituted proteins not only advances fundamental biological knowledge but also paves the way for innovative drug design strategies aimed at diseases linked to dysregulated phosphorylation events. Therefore, focusing on the reconstitution of STYX proteins holds promise for unlocking new therapeutic avenues in biomedical research.
