Analytical Data
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Gene name
SEPT10
- Application
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Alternative Names
FLJ11619; SEP10_HUMAN; SEPT 10; SEPT10; Septin 10; Septin-10
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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
Q9P0V9
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Expression Region
1-454 aa
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AA Sequence
MASSEVARHL LFQSHMATKT TCMSSQGSDD EQIKRENIRS LTMSGHVGFE SLPDQLVNRS IQQGFCFNIL CVGETGIGKS TLIDTLFNTN FEDYESSHFC PNVKLKAQTY ELQESNVQLK LTIVNTVGFG DQINKEESYQ PIVDYIDAQF EAYLQEELKI KRSLFTYHDS RIHVCLYFIS PTGHSLKTLD LLTMKNLDSK VNIIPVIAKA DTVSKTELQK FKIKLMSELV SNGVQIYQFP TDDDTIAKVN AAMNGQLPFA VVGSMDEVKV GNKMVKARQY PWGVVQVENE NHCDFVKLRE MLICTNMEDL REQTHTRHYE LYRRCKLEEM GFTDVGPENK PVSVQETYEA KRHEFHGERQ RKEEEMKQMF VQRVKEKEAI LKEAERELQA KFEHLKRLHQ EERMKLEEKR RLLEEEIIAF SKKKATSEIF HSQSFLATGS NLRKDKDRKN SNFL
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Molecular Weight
52.5 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
SEPT10, a member of the Septin protein family, plays a critical role in various cellular processes, including cytokinesis, cell division, and membrane dynamics. The study of SEPT10 has gained attention due to its involvement in cancer biology and neurodegenerative diseases, where altered expression of Septins has been associated with tumor progression and cellular dysfunction. SEPT10 is known to form hetero-oligomeric complexes with other Septins, contributing to the formation of filaments that participate in the regulation of cellular structures such as the actin cytoskeleton and microtubules. Understanding the biochemical properties and functional roles of SEPT10 is essential for elucidating its mechanisms in health and disease. Recent advancements in structural biology and protein engineering have enabled researchers to explore SEPT10's interactions at a molecular level, aiming to develop therapeutic strategies that target SEPT10-related pathways. Given its potential as a biomarker and therapeutic target, ongoing research on SEPT10 is crucial for uncovering novel insights into its role in maintaining cellular integrity and its implications in pathologies.
