Analytical Data
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Gene name
SEPTIN2
- Application
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Alternative Names
SEPTIN2；DIFF6；KIAA0158；NEDD5；Septin-2
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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
Q15019
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Expression Region
1-361aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSKQQPTQFINPETPGYVGFANLPNQVHRK SVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVISGAAEKIERTVQ IEASTVEIEERGVKLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYL HDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPV IAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDFKEQTRL LKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTML ITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELR RMQEMIARMQAQMQMQMQGGDGDGGALGHHV
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Molecular Weight
44 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, a member of the septin family of GTP-binding proteins, plays a critical role in various cellular processes, including cytokinesis, cell division, and the establishment of cellular architecture. These proteins can form hetero-oligomeric complexes and are involved in the regulation of membrane dynamics and the organization of the cytoskeleton. Specifically, SEPTIN2 has emerged as a key player in cytokinesis, where it aids in the formation of the septin ring—a structure crucial for the successful division of cells. Dysregulation of SEPTIN2 has been implicated in numerous diseases, including cancer and neurodegenerative disorders, highlighting its potential as a therapeutic target. Research efforts have focused on recombinantly expressing SEPTIN2 to elucidate its structural properties and interactions with other proteins. By studying its biochemical characteristics and cellular localization, researchers aim to define its functional roles and the molecular mechanisms by which it contributes to cell cycle regulation and disease progression. Understanding SEPTIN2 through recombinant protein studies not only enhances our knowledge of its biological importance but also opens avenues for developing novel therapeutic strategies aimed at modulating its activity in pathological conditions. As interest in the septins continues to grow, the exploration of SEPTIN2 provides valuable insights into the intricate interplay between cytoskeletal dynamics and cellular function.
