Analytical Data
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Gene name
ATG3
- Application
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Alternative Names
Autophagy-related protein 3 ;APG3-like ;hApg3;Protein PC3-96
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NT62
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Expression Region
1-314aa
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Molecular Weight
51.9 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
ATG3, a key protein in the autophagy process, plays a fundamental role in the formation of autophagosomes, which are essential for cellular homeostasis and the degradation of damaged organelles and proteins. It is a member of the autophagy-related (ATG) protein family and functions as an E2-like enzyme, facilitating the conjugation of the ubiquitin-like protein LC3 to phosphatidylethanolamine (PE) during autophagosome formation. This conjugation is crucial for the maturation of autophagosomes and their subsequent fusion with lysosomes. Research has increasingly focused on ATG3 due to its implications in various physiological processes and disease states, including cancer, neurodegenerative disorders, and infections. Dysregulation of autophagy, where ATG3's activity may be altered, has been associated with the pathogenesis of these diseases, making ATG3 an attractive target for therapeutic interventions. Furthermore, understanding the mechanistic details of ATG3’s interactions with other autophagy-related proteins can provide insights into the broader regulatory networks of autophagy, potentially uncovering new avenues for drug development and treatment strategies. As such, ongoing studies aim to delineate the structural features and functional dynamics of ATG3, identifying how modifications in its expression or activity could influence overall autophagic processes within cells. This increasing interest in ATG3 underscores its importance not only in basic cellular biology but also in its potential clinical applications, highlighting the need for continued investigation into this crucial protein's role within the autophagic machinery.
