Analytical Data
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Gene name
SEPT6
- Application
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Alternative Names
SEPTIN6;KIAA0128;SEP2;SEPT6;Septin-6
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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
Q14141
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Expression Region
1-434aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMAATDIARQVGEGCRTVPLAGHVGFDS LPDQLVNKSVSQGFCFNILCVGETGLGKSTLMDTLFNTKFEGEPATHTQP GVQLQSNTYDLQESNVRLKLTIVSTVGFGDQINKEDSYKPIVEFIDAQFE AYLQEELKIRRVLHTYHDSRIHVCLYFIAPTGHSLKSLDLVTMKKLDSKV NIIPIIAKADAISKSELTKFKIKITSELVSNGVQIYQFPTDDESVAEING TMNAHLPFAVIGSTEELKIGNKMMRARQYPWGTVQVENEAHCDFVKLREM LIRVNMEDLREQTHTRHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAK RNEFLGELQKKEEEMRQMFVQRVKEKEAELKEAEKELHEKFDRLKKLHQD EKKKLEDKKKSLDDEVNAFKQRKTAAELPQSQGSQAGGSQTLKRDKEKKN NPWLCTE
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Molecular Weight
52 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
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Protein Description
SEPT6, a member of the septin family of proteins, plays a crucial role in various cellular processes, including cell division, cytoskeletal organization, and membrane dynamics. Septins are characterized by their ability to form hetero-oligomeric complexes that contribute to the formation of filamentous structures, acting as scaffolding components in the cytoplasm. Research into SEPT6 has gained momentum due to its involvement in significant pathological conditions, including cancer and neurodegenerative disorders. Studies have shown that SEPT6 interacts with a variety of cellular partners, influencing cell signaling pathways and contributing to the regulation of essential cellular functions. Moreover, the dysregulation of SEPT6 has been linked to tumorigenesis, making it a potential biomarker for cancer progression and a target for therapeutic interventions. Recent advances in structural biology techniques, such as cryo-electron microscopy and X-ray crystallography, have provided insights into the molecular architecture of SEPT6 and its complexes, paving the way for the development of novel drugs that can modulate its activity. Overall, the ongoing exploration of SEPT6 and its functional implications in health and disease underscores its significance in cellular biology and its potential as a therapeutic target.
