Analytical Data
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Gene name
SEPT2
- 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
MSKQQPTQFINPETPGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRRMQEMIARMQAQMQMQMQGGDGDGGALGHHV
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Molecular Weight
57.5kDa
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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
SEPT2 (Septin 2) is a member of the septin family of GTP-binding proteins, which play a crucial role in various cellular processes, including cytoskeletal organization, cell division, and the formation of membranous structures. The study of SEPT2 has gained traction due to its involvement in essential cellular functions and its potential implications in human diseases, such as cancer and neurodegenerative disorders. SEPT2 is known to form hetero-oligomeric complexes with other septins, contributing to the integrity and functionality of cellular frameworks. Abnormalities in septin expression and function have been associated with disrupted cell signaling pathways, leading to abnormal cell proliferation and migration. Additionally, SEPT2's role in the formation of septin-based structures, such as midbody and ring-like formations during cytokinesis, highlights its importance in ensuring proper cell division. Recent research efforts have focused on elucidating the structural dynamics of SEPT2, its interaction with other proteins, and its regulatory mechanisms within the cell. Understanding these aspects could provide insights into the molecular underpinnings of associated diseases and offer potential avenues for therapeutic interventions. Therefore, the study of SEPT2 and its recombinant protein forms is pivotal in advancing our comprehension of cell biology and developing strategies to target septin-related pathologies.
