Analytical Data
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Gene name
AP4s1
- Application
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Alternative Names
AP4s1;AP-4 complex subunit sigma-1
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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
Q9Y587
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Expression Region
1-144aa
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AA Sequence
MIKFFLMVNKQGQTRLSKYYEHVDINKRTLLETEVIKSCLSRSNEQCSFIEYKDFKLIYRQYAALFIVVGVNDTENEMAIYEFIHNFVEVLDEYFSRVSELDIMFNLDKVHIILDEMVLNGCIVETNRARILAPLLILDKMSES
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Molecular Weight
17 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
AP4S1, also known as AP-4 sigma subunit, plays a critical role in the assembly and function of adaptor protein complexes, particularly clathrin-coated vesicles, which are essential for intracellular trafficking. Research into AP4S1 has gained momentum due to its involvement in various cellular processes, including endocytosis, receptor sorting, and trans-Golgi network function. Mutations or dysregulation of AP4S1 have been implicated in neurodevelopmental disorders and other pathologies, highlighting its significance in maintaining normal cellular function. Understanding the structure and function of AP4S1 is vital for elucidating its role in membrane trafficking and identifying potential therapeutic targets for diseases associated with its dysfunction. Recent advances in recombinant protein technology have facilitated the study of AP4S1, allowing for detailed investigations into its biochemical properties, interaction with other protein complexes, and the impact of genetic variations. These insights are crucial for developing strategies to address disorders linked to AP4S1 mutations, thereby advancing our knowledge of cellular mechanisms underlying both health and disease.











