Analytical Data
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Gene name
SEPT5
- Application
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Alternative Names
CDCREL; CDCREL-1; CDCREL1; H5; PNUTL1; Peanut-Like 1; Cell division control-related protein 1
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Species
Human
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Source
E. coli
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Tag
N-His
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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
Ser77~Ser323
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Molecular Weight
30kDa
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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
SEPT5, also known as Septin 5, is a member of the septin family of GTP-binding proteins that play crucial roles in various cellular processes, including cell division, cytoskeletal organization, and vesicle trafficking. This protein is particularly interesting due to its involvement in the formation of septin complexes, which are thought to function as scaffolding components in the assembly of cellular structures. Research has shown that SEPT5 is implicated in several physiological processes, such as cell cycle regulation and neuronal function, and has been linked to various diseases, including cancer and neurodegenerative disorders. The study of SEPT5 has gained momentum in recent years as scientists explore its role in disease mechanisms and potential as a therapeutic target. Investigating the structure and function of SEPT5, particularly in the context of its interactions with other cellular proteins and its regulatory mechanisms, is crucial for understanding its biological significance. Advancements in techniques such as X-ray crystallography and cryo-electron microscopy have enabled researchers to elucidate the molecular details of SEPT5, paving the way for novel therapeutic strategies targeting septin-associated pathways. Furthermore, the modulation of SEPT5 activity is being explored for its potential to influence tumorigenesis and neurodegenerative processes, making it a focal point for future research in cellular biology and medicine.
