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Cardiolipin interaction with various Atg8 (show GABARAPL2 ELISA Kits) human orthologs, namely LC3B (show MAP1LC3B ELISA Kits), GABARAPL2 (show GABARAPL2 ELISA Kits) and GABARAP, was investigated.
Development of LC3 (show MAP1LC3A ELISA Kits)/GABARAP sensors containing a LIR (show CD300C ELISA Kits) and a hydrophobic domain to monitor autophagy.
GABRP (show GABRP ELISA Kits) plays an important role in placentation and this pathway may be a promising molecular target for the development of novel therapeutic strategies for preeclampsia.
KBTBD6 and KBTBD7 specifically bind to GABARAP proteins.GABARAP proteins mediate localized ubiquitylation of TIAM1 by CUL3 (show CUL3 ELISA Kits).
Data show that WAC (show WAC ELISA Kits) directly binds to GM130 (show GOLGA2 ELISA Kits) and that this binding is required for autophagosome formation through interacting with GABARAP regulating its subcellular localization.
The interaction of GABARAP with Mulan-Ube2E3 supports the role of Mulan as an important regulator of mitophagy.
The FLCN (show FLCN ELISA Kits)-GABARAP association is modulated by the presence of either folliculin (show FLCN ELISA Kits)-interacting protein (FNIP)-1 (show FNIP1 ELISA Kits) or FNIP2 and further regulated by ULK1 (show ULK1 ELISA Kits).
A functional complementation of an lgg-1 null mutant with human GABARAP, its closer homolog showed that it localizes to autophagosomes and can rescue LGG-1 functions in the early embryo.
PLEKHM1 (show PLEKHM1 ELISA Kits) regulates autophagosome-lysosome fusion through homotypic fusion and protein sorting complex and LC3 (show MAP1LC3A ELISA Kits)/GABARAP proteins.
GABARBP dramatically inhibited VEGF (show VEGFA ELISA Kits)-induced endothelial cell proliferation, migration, and tube formation, as well as VEGFR-2 (show KDR ELISA Kits) phosphorylation in vitro.
DLG4/PSD95 (show DLG4 ELISA Kits) and GABARAP were analyzed using zebrafish embryos with morpholino knockdown system as a model organism.
Cells that lacked GABARAPs and mice that lacked Gate-16 (show GABARAPL2 ELISA Kits) alone were defective in the IFN-gamma-induced (show SAMHD1 ELISA Kits) clearance of vacuolar pathogens such as Toxoplasma. GABARAPs are uniquely required for antimicrobial host defense through cytosolic distribution of interferon (show IFNA ELISA Kits)-inducible GTPases.
Ablation of GABARAP inhibits tumor initiation and progression through enhancement of both antitumor immunity and cell death signaling.
Lipidation of the LC3 (show MAP1LC3A ELISA Kits)/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3 (show ATG3 ELISA Kits).
These results support the regulatory role of Bcl-2 (show BCL2 ELISA Kits) in autophagy and define GABARAP as a novel interaction partner involved in this intricate connection.
Results indicate that, compared with LC3 (show MAP1LC3A ELISA Kits), GABARAP is enriched in the axonal initial segments (AIS (show AR ELISA Kits)).
Gabarap functions in the immune system. It is involved in mitochondrial quality control in macrophages, and thus it influences Nlrp3 (show NLRP3 ELISA Kits) inflammasome-dependent inflammatory responses.
ATG8 (show MAP1LC3B ELISA Kits)-like proteins (MAP1LC3B (show MAP1LC3B ELISA Kits), GABARAP and GABARAPL1 (show GABARAPL1 ELISA Kits)) are novel interactors of MAPK15/ERK8 (show MAPK15 ELISA Kits), a MAP kinase (show MAPK1 ELISA Kits) involved in cell proliferation and transformation.
GABARAP/p62 complex is responsible for impairment of glomerular function and that it retards recovery from the effects of doxorubicin.
because of its stronger binding for hKOPR, GEC1 (show GABARAPL1 ELISA Kits) is able to be recruited by hKOPR sufficiently without membrane association via its C-terminal modification; however, du GABARAP appears to require C-terminal modifications to enhance KOPR expression.
Gamma-aminobutyric acid A receptors
GABA(A) receptor-associated protein
, gaba(a) receptor-associated protein
, gamma-aminobutyric acid receptor-associated protein
, gamma-aminobutyric acid receptor associated protein
, cerebelluar GABA-A receptor-associated protein
, GABA(A) receptor associated protein
, GABA-A receptor-associated protein
, gamma-aminobutyric acid reseptor associated protein