Analytical Data
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Gene name
AP1S3
- Application
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Alternative Names
Adaptor protein complex AP-1 subunit sigma-1C;Adaptor-related protein complex 1 subunit sigma-1C;Clathrin assembly protein complex 1 sigma-1C small chain;Golgi adaptor HA1/AP1 adaptin sigma-1C subunit;Sigma 1C subunit of AP-1 clathrin;Sigma-adaptin 1C;Sigma1C-adaptin
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96PC3
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Expression Region
1-104aa
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Molecular Weight
39.7 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
AP1S3, a component of the adaptor protein complex 1 (AP-1), plays a crucial role in intracellular trafficking, particularly in the sorting of proteins within the trans-Golgi network and endosomes. Its involvement in clathrin-mediated endocytosis and the transport of cargo proteins to lysosomes has garnered attention in recent years. Mutations in the AP1S3 gene have been linked to several human diseases, including neurodevelopmental disorders and immunodeficiencies, highlighting its significance in cellular function and human health. Understanding the structural and functional dynamics of AP1S3 is essential for elucidating its role in these disease mechanisms. Recent advances in structural biology techniques, such as cryo-electron microscopy and X-ray crystallography, have provided insights into the conformational changes and the interaction interfaces of AP1S3 with other protein complexes. Ongoing research aims to explore the regulatory mechanisms governing AP1S3 activity and its potential as a therapeutic target for diseases resulting from dysfunctional protein trafficking. Thus, the study of AP1S3 not only enhances our understanding of cellular processes but also opens avenues for novel medical interventions.
