Analytical Data
-
Gene name
SEPT6
- Application
-
Alternative Names
SEP2
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q14141
-
Expression Region
Asp87~Lys327
-
Molecular Weight
31.5kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
SEPT6, a member of the septin protein family, plays a critical role in various cellular processes, including cytokinesis, apoptosis, and the maintenance of cellular structure. Septins are GTP-binding proteins that assemble into heteromeric complexes, forming filaments that contribute to the formation of ring-like structures at the sites of cell division. Research into SEPT6 has gained momentum due to its involvement in key cellular functions and its potential implications in various diseases, including cancer and neurodegenerative disorders. Abnormalities in septin function and expression have been linked to tumorigenesis, making SEPT6 a target of interest for potential therapeutic strategies. By exploring the molecular mechanisms underlying SEPT6's role in the cell cycle and its interactions with other cytoskeletal components, researchers aim to elucidate its contributions to cell division and differentiation. Additionally, the study of SEPT6 as a potential biomarker for certain cancers is ongoing, as its expression levels may correlate with tumor progression and patient prognosis. Understanding the structure, function, and regulatory mechanisms of SEPT6 through recombinant protein studies can provide valuable insights into its biological significance and pave the way for innovative approaches in cancer treatment and drug design.
