Analytical Data
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Gene name
SEPT11
- Application
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Alternative Names
SEP11_HUMAN; SEPT 11; Sept11; Septin-11; Septin11
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NVA2
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Expression Region
2-429 aa
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AA Sequence
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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Molecular Weight
49.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
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.
