Analytical Data
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Gene name
SEPT5
- Application
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Alternative Names
SEPTIN5;PNUTL1;SEPT5;Septin-5
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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
Q99719
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Expression Region
1-369aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMSTGLRYKSKLATPEDKQDIDKQYVGF ATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVHSLFLTDLYKDRKLLS AEERISQTVEILKHTVDIEEKGVKLKLTIVDTPGFGDAVNNTECWKPITD YVDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPVDVGFMKA LHEKVNIVPLIAKADCLVPSEIRKLKERIREEIDKFGIHVYQFPECDSDE DEDFKQQDRELKESAPFAVIGSNTVVEAKGQRVRGRLYPWGIVEVENQAH CDFVKLRNMLIRTHMHDLKDVTCDVHYENYRAHCIQQMTSKLTQDSRMES PIPILPLPTPDAETEKLIRMKDEELRRMQEMLQRMKQQMQDQ
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Molecular Weight
45 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
SEPT5, a member of the septin family of GTP-binding proteins, plays a crucial role in various cellular processes, including cytokinesis, cell division, and cytoskeletal organization. The study of SEPT5 has gained significant attention due to its involvement in neurobiology, particularly in synaptic function and neuronal development. Abnormalities in SEPT5 expression and function have been linked to several diseases, including neurodegenerative disorders and cancers, highlighting its potential as a therapeutic target. Researchers have focused on the structural properties and functional dynamics of SEPT5, utilizing advanced techniques such as cryo-electron microscopy and x-ray crystallography to elucidate its interactions with other proteins and cellular components. Furthermore, understanding the regulation of SEPT5 activity in response to cellular signals is essential for unveiling its role in pathophysiological conditions. This research not only contributes to the fundamental knowledge of septin biology but also opens avenues for the development of novel strategies for disease intervention, showcasing the importance of SEPT5 in both health and disease.
