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AB172826

Recombinant Human ATG4A protein

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Recombinant Human ATG4A protein is a Human Full Length protein, in the 1 to 398 aa range, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.

View Alternative Names

APG4A, AUTL2, ATG4A, Cysteine protease ATG4A, AUT-like 2 cysteine endopeptidase, Autophagy-related cysteine endopeptidase 2, Autophagy-related protein 4 homolog A, Autophagin-2, HsAPG4A, hAPG4A

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, HPLC

applications

Biologically active

No

Accession

Q8WYN0

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: 100% PBS

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "HPLC": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMESVLSKYEDQITIFTDYLEEYPDTDELVWILGKQHLLKTEKSKLLSDISARLWFTYRRKFSPIGGTGPSSDAGWGCMLRCGQMMLAQALICRHLGRDWSWEKQKEQPKEYQRILQCFLDRKDCCYSIHQMAQMGVGEGKSIGEWFGPNTVAQVLKKLALFDEWNSLAVYVSMDNTVVIEDIKKMCRVLPLSADTAGDRPPDSLTASNQSKGTSAYCSAWKPLLLIVPLRLGINQINPVYVDAFKECFKMPQSLGALGGKPNNAYYFIGFLGDELIFLDPHTTQTFVDTEENGTVNDQTFHCLQSPQRMNILNLDPSVALGFFCKEEKDFDNWCSLVQKEILKENLRMFELVQKHPSHWPPFVPPAKPEVTTTGAEFIDSTEQLEEFDLEEDFEILSV","proteinLength":"Full Length","predictedMolecularWeight":"45 kDa","actualMolecularWeight":null,"aminoAcidEnd":398,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q8WYN0","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

ATG4A also known as Autophagin 1 is a cysteine protease with a mass of approximately 52 kDa. It plays a critical role in the autophagy pathway by cleaving LC3 and other Atg8 homologs facilitating their conjugation to phosphatidylethanolamine on the autophagosome membrane. This protein is expressed in various tissues including the liver and skeletal muscle indicating its involvement in diverse physiological processes.
Biological function summary

ATG4A contributes essential functions to cellular homeostasis by participating in autophagosome formation. As part of the group of Atg proteins it collaborates with other members to modulate the autophagy machinery. ATG4A's enzymatic activity provides the necessary steps for processing LC3 transforming it into a form that allows lipidation and incorporation into autophagic vesicles.

Pathways

ATG4A is integral to the autophagy pathway a catabolic process important for cell survival under stress conditions. It interacts with proteins such as ATG7 and ATG3 within this pathway playing a significant role in the early stages of autophagosome maturation. The interactions ensure proper recycling of cellular materials and its efficient function impact cellular metabolism and stress responses.

Disruptions in ATG4A function have been linked to neurodegenerative diseases and cancer. Aberrant autophagy processes involving ATG4A can lead to protein aggregation disorders such as Alzheimer’s disease where proper proteostasis is compromised. Also in certain cancers altered ATG4A activity can influence tumor growth often through modulation of metabolic pathways and interactions with proteins like Beclin 1 which regulate autophagic responses.
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Specifications

Form

Liquid

Additional notes

Purity is greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. Supplied as a 0.2 µM filtered solution.

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General info

Function

Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed : 12473658, PubMed : 15169837, PubMed : 17347651, PubMed : 21177865, PubMed : 21245471, PubMed : 22302004, PubMed : 32732290). The protease activity is required for proteolytic activation of ATG8 family proteins : cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine (PubMed : 12473658, PubMed : 15169837, PubMed : 17347651, PubMed : 21177865, PubMed : 21245471, PubMed : 22302004). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (PubMed : 12473658, PubMed : 15169837, PubMed : 17347651, PubMed : 21177865, PubMed : 21245471, PubMed : 22302004). Preferred substrate is GABARAPL2 followed by MAP1LC3A and GABARAP (PubMed : 12473658, PubMed : 15169837, PubMed : 17347651, PubMed : 21177865, PubMed : 21245471, PubMed : 22302004). Protease activity is also required to counteract formation of high-molecular weight conjugates of ATG8 proteins (ATG8ylation) : acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3 (PubMed : 31315929, PubMed : 33773106). In addition to the protease activity, also mediates delipidation of ATG8 family proteins (PubMed : 29458288, PubMed : 33909989). Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (PubMed : 29458288, PubMed : 33909989). Compared to ATG4B, the major protein for proteolytic activation of ATG8 proteins, shows weaker ability to cleave the C-terminal amino acid of ATG8 proteins, while it displays stronger delipidation activity (PubMed : 29458288). Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins : acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy (PubMed : 33773106).

Sequence similarities

Belongs to the peptidase C54 family.

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Product protocols

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Target data

Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed : 12473658, PubMed : 15169837, PubMed : 17347651, PubMed : 21177865, PubMed : 21245471, PubMed : 22302004, PubMed : 32732290). The protease activity is required for proteolytic activation of ATG8 family proteins : cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine (PubMed : 12473658, PubMed : 15169837, PubMed : 17347651, PubMed : 21177865, PubMed : 21245471, PubMed : 22302004). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (PubMed : 12473658, PubMed : 15169837, PubMed : 17347651, PubMed : 21177865, PubMed : 21245471, PubMed : 22302004). Preferred substrate is GABARAPL2 followed by MAP1LC3A and GABARAP (PubMed : 12473658, PubMed : 15169837, PubMed : 17347651, PubMed : 21177865, PubMed : 21245471, PubMed : 22302004). Protease activity is also required to counteract formation of high-molecular weight conjugates of ATG8 proteins (ATG8ylation) : acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3 (PubMed : 31315929, PubMed : 33773106). In addition to the protease activity, also mediates delipidation of ATG8 family proteins (PubMed : 29458288, PubMed : 33909989). Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (PubMed : 29458288, PubMed : 33909989). Compared to ATG4B, the major protein for proteolytic activation of ATG8 proteins, shows weaker ability to cleave the C-terminal amino acid of ATG8 proteins, while it displays stronger delipidation activity (PubMed : 29458288). Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins : acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy (PubMed : 33773106).
See full target information ATG4A
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Advanced Validation

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