Analytical Data
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Gene name
ATG3
- Application
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Alternative Names
ATG3；APG3；APG3L；；Ubiquitin-like-conjugating enzyme ATG3
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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
Q9NT62
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Expression Region
1-314aa
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AA Sequence
MQNVINTVKGKALEVAEYLTPVLKESKFKETGVITPEEFVAAGDHLVHHC PTWQWATGEELKVKAYLPTGKQFLVTKNVPCYKRCKQMEYSDELEAIIEE DDGDGGWVDTYHNTGITGITEAVKEITLENKDNIRLQDCSALCEEEEDED EGEAADMEEYEESGLLETDEATLDTRKIVEACKAKTDAGGEDAILQTRTY DLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMYEDISQDHVKKTVTIENH PHLPPPPMCSVHPCRHAEVMKKIIETVAEGGGELGVHMYL LIFLKFVQAVIPTIEYDYTR HFTM
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Molecular Weight
33 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 crucial component of the autophagy machinery, plays a significant role in the formation of autophagosomes, which are vital for cellular degradation and recycling processes. Autophagy is an essential cellular process that helps maintain homeostasis by removing damaged organelles and misfolded proteins, thereby preventing the development of various diseases, including neurodegenerative disorders, cancer, and infections. Research on ATG3 has gained momentum due to its involvement in the ubiquitin-like conjugation systems that facilitate the lipidation of LC3, a core protein in autophagosome formation. Understanding the functional dynamics of ATG3 offers insights into the mechanisms underlying autophagy regulation, cellular stress responses, and the potential development of therapeutic strategies targeting autophagy-dependent pathways. Given that dysregulation of autophagy is associated with several diseases, the study of ATG3 and its interactions with other autophagy-related proteins is pivotal in deciphering its role in health and disease. Current studies are exploring the structural characteristics of ATG3, its regulatory mechanisms, and its potential as a target for drug development in diseases where autophagy is altered. This area of research not only enhances our understanding of fundamental cellular processes but also holds promise for innovative therapeutic approaches.
