Analytical Data
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Gene name
SEPT1
- Application
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Alternative Names
SEPTIN1; SEPT1; Septin-1
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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
A5PJU9
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Expression Region
1-367 aa
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AA Sequence
MDKEYVGFAA LPNQLHRKSV KKGFDFTLMV AGESGLGKST LINSLFLTNL YEDRQIPEAS ARLTQTLTIE RRGVEIEEGG IKVKLTVVDT PGFGDSVDCS DCWLPVVRFI EEQFEQYLRD ESGLNRKNIQ DSRVHCCLYF ISPFGRGLRP LDVAFLRAVH EKVNIIPVIG KADALMPKET QALKQKIREQ LKEEEINIYQ FPECDSDEDE DFKRQDAEMK ESIPFAVVGS CEVVRDGGPR PVRGRHYSWG TVEVENPHHC DFLNLRRMLV QTHLQDLKEV THDLLYEGYR ARCLQSLARP GARDRASRSK LSRQSATEIP LPMLPLADTE KLIREKDEEL RRMQEMLEKM QAQMQLSQAQ GEQSDAL
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Molecular Weight
41.9 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
SEPT1 ( septin 1) is a member of the septin family of GTP-binding proteins, which play a crucial role in various cellular processes, including cytokinesis, apoptosis, and the formation of cellular structures. The study of SEPT1 has gained attention due to its involvement in the regulation of cell division and its potential link to several diseases, including cancer. Abnormal SEPT1 expression has been observed in various tumor types, suggesting that it may serve as a biomarker for cancer progression. Research has indicated that SEPT1 interacts with other cytoskeletal proteins and is involved in maintaining cell shape and integrity. Understanding the molecular mechanisms of SEPT1, including its structure and function in cellular pathways, is essential for developing targeted therapies. Additionally, as a part of the septin complex, SEPT1 may also contribute to the formation of higher-order structures that are crucial for cellular organization. Thus, ongoing research is focused on the biochemical characterization, spatial dynamics, and potential therapeutic applications of SEPT1, aiming to unveil its role in health and disease and to identify novel strategies for intervention in malignant processes.
