Analytical Data
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基因名
SEPT11
- Application
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别名
SEP11_HUMAN; SEPT 11; Sept11; Septin-11; Septin11
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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
Q9NVA2
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表达区间
2-429 aa
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氨基酸序列
AVAVGRPSN EELRNLSLSG HVGFDSLPDQ LVNKSTSQGF CFNILCVGET GIGKSTLMDT LFNTKFESDP ATHNEPGVRL KARSYELQES NVRLKLTIVD TVGFGDQINK DDSYKPIVEY IDAQFEAYLQ EELKIKRSLF NYHDTRIHAC LYFIAPTGHS LKSLDLVTMK KLDSKVNIIP IIAKADTIAK NELHKFKSKI MSELVSNGVQ IYQFPTDEET VAEINATMSV HLPFAVVGST EEVKIGNKMA KARQYPWGVV QVENENHCDF VKLREMLIRV NMEDLREQTH TRHYELYRRC KLEEMGFKDT DPDSKPFSLQ ETYEAKRNEF LGELQKKEEE MRQMFVMRVK EKEAELKEAE KELHEKFDLL KRTHQEEKKK VEDKKKELEE EVNNFQKKKA AAQLLQSQAQ QSGAQQTKKD KDKKNASFT
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分子量
49.3 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
SEPT11, a member of the Septin protein family, has garnered significant attention in recent years due to its pivotal role in various cellular processes, including cytokinesis, cytoskeletal organization, and the maintenance of cell shape. Septins are GTP-binding proteins that assemble into filamentous structures, contributing to the formation of scaffolds that organize cellular components. Research on SEPT11 is driven by its involvement in critical biological functions and its potential implications in diseases, particularly cancers and neurodegenerative disorders. Dysregulation of septin function has been linked to abnormal cell division and tumorigenesis, making SEPT11 a candidate for therapeutic intervention. Additionally, understanding its structure and interaction with other cellular proteins can provide insights into the mechanisms underlying cell-cycle regulation and cellular homeostasis. As scientists continue to explore the fundamental roles of SEPT11 in cell biology, its potential as a biomarker for disease progression and a target for novel treatments is increasingly recognized, paving the way for future research and therapeutic strategies.
