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Gamma-aminobutyric acid A receptors [GABA(A) receptors] are ligand-gated chloride channels that mediate inhibitory neurotransmission. Additionally we are shipping GABA(A) Receptor-Associated Protein Antibodies (181) and GABA(A) Receptor-Associated Protein Kits (1) and many more products for this protein.
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Human GABARAP Protein expressed in Escherichia coli (E. coli) - ABIN666937
Stangler, Mayr, Willbold: Solution structure of human GABA(A) receptor-associated protein GABARAP: implications for biolgoical funcrion and its regulation. in The Journal of biological chemistry 2002
KBTBD6 and KBTBD7 specifically bind to GABARAP proteins.GABARAP proteins mediate localized ubiquitylation of TIAM1 (show TIAM1 Proteins) by CUL3 (show CUL3 Proteins).
Data show that WAC (show WAC Proteins) directly binds to GM130 (show GOLGA2 Proteins) and that this binding is required for autophagosome formation through interacting with GABARAP regulating its subcellular localization.
The interaction of GABARAP with Mulan (show MUL1 Proteins)-Ube2E3 (show UBE2E3 Proteins) supports the role of Mulan (show MUL1 Proteins) as an important regulator of mitophagy.
The FLCN (show FLCN Proteins)-GABARAP association is modulated by the presence of either folliculin (show FLCN Proteins)-interacting protein (FNIP)-1 or FNIP2 (show FNIP2 Proteins) and further regulated by ULK1 (show ULK1 Proteins).
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 Proteins) regulates autophagosome-lysosome fusion through homotypic fusion and protein sorting complex and LC3 (show MAP1LC3A Proteins)/GABARAP proteins.
GABARBP dramatically inhibited VEGF (show VEGFA Proteins)-induced endothelial cell proliferation, migration, and tube formation, as well as VEGFR-2 (show KDR Proteins) phosphorylation in vitro.
knockdown of LC3B (show MAP1LC3B Proteins) but not GABARAPs resulted in significant accumulation of p62/Sqstm1 (show SQSTM1 Proteins), one of the selective substrates for autophagy
These results support the regulatory role of Bcl-2 (show BCL2 Proteins) in autophagy and define GABARAP as a novel interaction partner involved in this intricate connection.
Taken together, our results indicate that GABARBP can regulate the pro-apoptotic activity of cisplatin via the upregulation of p53 (show TP53 Proteins) expression.
DLG4/PSD95 (show DLG4 Proteins) and GABARAP were analyzed using zebrafish embryos with morpholino knockdown system as a model organism.
Lipidation of the LC3 (show MAP1LC3A Proteins)/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3 (show ATG3 Proteins).
Results indicate that, compared with LC3 (show MAP1LC3A Proteins), GABARAP is enriched in the axonal initial segments (AIS (show AR Proteins)).
Gabarap functions in the immune system. It is involved in mitochondrial quality control in macrophages, and thus it influences Nlrp3 (show NLRP3 Proteins) inflammasome-dependent inflammatory responses.
ATG8 (show MAP1LC3B Proteins)-like proteins (MAP1LC3B (show MAP1LC3B Proteins), GABARAP and GABARAPL1 (show GABARAPL1 Proteins)) are novel interactors of MAPK15/ERK8 (show MAPK15 Proteins), a MAP kinase (show MAPK1 Proteins) 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 Proteins) 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.
In GABARAP-deficient mice renal NaPi-IIa (show SLC34A1 Proteins) is up-regulation and intestinal NaPi-IIb (show SLC34A2 Proteins) is downregulated.
Results suggest that lysosomal turnover of GABARAP-PL is activated during the differentiation of C2C12 cells to myotubes without inactivation of the mTor (show FRAP1 Proteins) kinase-signaling pathway.
the organization of extrasynaptic GABA(A) receptors and GABARAP may provide a range of distinct inhibitory currents in the brain
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