Analytical Data
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Gene name
SEPT8
- Application
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Alternative Names
SEPTIN8; KIAA0202; SEPT8; Septin-8
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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
Q92599
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Expression Region
2-483 aa
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AA Sequence
AATDLERFS NAEPEPRSLS LGGHVGFDSL PDQLVSKSVT QGFSFNILCV GETGIGKSTL MNTLFNTTFE TEEASHHEAC VRLRPQTYDL QESNVQLKLT IVDAVGFGDQ INKDESYRPI VDYIDAQFEN YLQEELKIRR SLFDYHDTRI HVCLYFITPT GHSLKSLDLV TMKKLDSKVN IIPIIAKADT ISKSELHKFK IKIMGELVSN GVQIYQFPTD DEAVAEINAV MNAHLPFAVV GSTEEVKVGN KLVRARQYPW GVVQVENENH CDFVKLREML IRVNMEDLRE QTHSRHYELY RRCKLEEMGF QDSDGDSQPF SLQETYEAKR KEFLSELQRK EEEMRQMFVN KVKETELELK EKERELHEKF EHLKRVHQEE KRKVEEKRRE LEEETNAFNR RKAAVEALQS QALHATSQQP LRKDKDKKNR SDIGAHQPGM SLSSSKVMMT KASVEPLNCS SWWPAIQCCS CLVRDATWRE GFL
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Molecular Weight
55.7 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
SEPT8, a member of the septin family of GTP-binding proteins, plays a crucial role in various cellular processes, including cytokinesis, cytoskeletal organization, and membrane dynamics. Research in recent years has revealed that SEPT8 is involved in critical biological functions and possibly in the development of various diseases, such as neurodegenerative disorders and cancer. Its role in cellular compartmentalization and the formation of septin fibers has sparked interest in understanding how SEPT8 contributes to cellular architecture. Furthermore, the modulation of SEPT8 levels has been implicated in cell proliferation and differentiation, making it a potential target for therapeutic interventions. As scientists continue to explore the structural and functional aspects of SEPT8, the focus on the recombinant production of this protein has gained momentum. By employing advanced techniques in protein engineering, researchers aim to elucidate the functional properties of SEPT8 and its interactions with other cellular components. Enhanced understanding of SEPT8's structure through recombinant protein studies may lead to breakthroughs in developing innovative strategies for disease treatment. Thus, the investigation of SEPT8 as a recombinant protein represents a significant advancement in cell biology and medicine, paving the way for novel insights into cellular mechanisms and potential therapeutic applications.
