Anti-ATG4B antibody [HL2348],Abcam,AB317205

Host

Rabbit

Reactivity

Human, Mouse, Rat

Application

IHC-P, WB

Platform ID

BAB530545889

Abcam

Headquarters

Discovery Drive Cambridge Biomedical Campus Cambridge CB2 0AX UK

Contact

Tel: +44 (0)1223 696000
Fax: +44 (0)1223 215 215

Product Specifications
Scientific Background

Specifications

NameAnti-ATG4B antibody [HL2348]
Cat. No.AB317205
HostRabbit
IsotypeIgG
ReactivityHuman, Mouse, Rat
ApplicationIHC-P, WB
ClonalityMonoclonal
Clone NumberHL2348
ImmunogenRecombinant Fragment Protein within Human ATG4B.
Appearance/FormLiquid
ShippingBlue Ice
FormulationpH: 7.4 Constituents: PBS
Storage-20°C
Regulatory StatusResearch Use Only

Scientific Background

Target data Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed : 15169837, PubMed : 15187094, PubMed : 17347651, PubMed : 19322194, PubMed : 21177865, PubMed : 22302004, PubMed : 26378241, PubMed : 27527864, PubMed : 28633005, PubMed : 28821708, PubMed : 29232556, PubMed : 30076329, PubMed : 30443548, PubMed : 30661429). Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy (PubMed : 33773106, PubMed : 33909989). The protease activity is required for proteolytic activation of ATG8 family proteins : cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine (PubMed : 15169837, PubMed : 15187094, PubMed : 17347651, PubMed : 19322194, PubMed : 20818167, PubMed : 21177865, PubMed : 22302004, PubMed : 27527864, PubMed : 28287329, PubMed : 28633005, PubMed : 29458288, PubMed : 30661429). 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 : 15169837, PubMed : 15187094, PubMed : 17347651, PubMed : 19322194, PubMed : 21177865, 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 : 15187094, PubMed : 19322194, PubMed : 28633005, PubMed : 29458288, PubMed : 32686895, PubMed : 33909989). Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (PubMed : 15187094, PubMed : 19322194, PubMed : 29458288, PubMed : 32686895, PubMed : 33909989). Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed : 33909989). Compared to other members of the family (ATG4A, ATG4C or ATG4C), constitutes the major protein for proteolytic activation of ATG8 proteins, while it displays weaker delipidation activity than other ATG4 paralogs (PubMed : 29458288, PubMed : 30661429). 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 ATG4B

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