Analytical Data
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Gene name
SEPTIN2
- Application
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Alternative Names
Neural precursor cell expressed developmentally down-regulated protein 5 Short name: NEDD-5
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15019
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Expression Region
1-361aa
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Molecular Weight
57.5 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
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Protein Description
Septin2 is a member of the septin family of GTP-binding proteins, which are essential for various cellular processes, including cytokinesis, cell division, and the establishment of cell polarity. Research into Septin2 has gained momentum due to its critical role in the organization of the cytoskeleton and its involvement in the formation of septin filament structures, which contribute to the stability and integrity of cellular compartments. Moreover, septins, including Septin2, have been implicated in several pathological conditions, including cancer, neurodegenerative diseases, and bacterial infections, highlighting their potential as therapeutic targets. Recent advances in recombinant protein technology have enabled the production of high-purity Septin2 for in-depth studies, allowing researchers to explore its biochemical properties, interaction partners, and functional roles within cells. Furthermore, understanding the molecular mechanisms by which Septin2 operates could provide insights into the regulation of cell morphology and division, opening avenues for novel interventions in diseases where septin dysfunction is a contributing factor. Overall, the study of recombinant Septin2 protein represents a significant step in elucidating the complex roles of septins in health and disease.
