Analytical Data
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Gene name
ATG4C
- Application
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Alternative Names
ATG4C；APG4C；AUTL1；AUTL3；Cysteine protease ATG4C
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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
Q96DT6
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Expression Region
1-458aa
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AA Sequence
MEATGTDEVD KLKTKFISAW NNMKYSWVLK TKTYFSRNSP VLLLGKCYHF KYEDEDKTLP AESGCTIEDH VIAGNVEEFR KDFISRIWLT YREEFPQIEG SALTTDCGWG CTLRTGQMLL AQGLILHFLG RAWTWPDALN IENSDSESWT SHTVKKFTAS FEASLSGERE FKTPTISLKE TIGKYSDDHE MRNEVYHRKI ISWFGDSPLA LFGLHQLIEY GKKSGKKAGD WYGPAVVAHI LRKAVEEARH PDLQGITIYV AQDCTVYNSD VIDKQSASMT SDNADDKAVI ILVPVRLGGE RTNTDYLEFV KGILSLEYCV GIIGGKPKQS YYFAGFQDDS LIYMDPHYCQ SFVDVSIKDF PLETFHCPSP KKMSFRKMDP SCTIGFYCRN VQDFKRASEE ITKMLKFSSK EKYPLFTFVN GHSRDYDFTS TTTNEEDLFS EDEKKQLKRF STEEFVLL
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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
ATG4C, a member of the ATG4 family of cysteine proteases, plays a pivotal role in the autophagy process by regulating the lipidation status of LC3, a key protein in autophagosome formation. Research on ATG4C has gained momentum due to its implications in various cellular processes and disease states, including cancer, neurodegenerative disorders, and infection responses. Unlike other members of the ATG4 family, ATG4C exhibits distinct substrate specificity and regulatory mechanisms, making it a unique target for therapeutic interventions. Recent studies have indicated that ATG4C not only contributes to the modulation of autophagic flux but also participates in the regulation of mitochondrial dynamics and cellular stress responses. Understanding the structure-function relationships of ATG4C through recombinant protein studies is essential for elucidating its role in autophagy and potential as a drug target. Insights gained from studying ATG4C can pave the way for novel strategies to manipulate autophagy in disease contexts, potentially enhancing disease treatment and prevention approaches. Thus, the comprehensive characterization of ATG4C as a recombinant protein is critical for advancing our knowledge of autophagy-related mechanisms and their relevance in health and disease.
