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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 Proteins (26) and GABA(A) Receptor-Associated Protein Kits (1) and many more products for this protein.
Showing 10 out of 184 products:
Human Polyclonal GABARAP Primary Antibody for IHC, WB - ABIN349993
Boileau, Pearce, Czajkowski: Tandem subunits effectively constrain GABAA receptor stoichiometry and recapitulate receptor kinetics but are insensitive to GABAA receptor-associated protein. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2005
Show all 6 references for ABIN349993
Human Polyclonal GABARAP Primary Antibody for IF, IHC (p) - ABIN388564
Knight, Harris, McAlister, Phelan, Geddes, Moss, Driscoll, Keep: The X-ray crystal structure and putative ligand-derived peptide binding properties of gamma-aminobutyric acid receptor type A receptor-associated protein. in The Journal of biological chemistry 2002
Show all 3 references for ABIN388564
Cow (Bovine) Polyclonal GABARAP Primary Antibody for WB - ABIN2784489
Kawaguchi, Hirano: Sustained structural change of GABA(A) receptor-associated protein underlies long-term potentiation at inhibitory synapses on a cerebellar Purkinje neuron. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2007
Human Polyclonal GABARAP Primary Antibody for WB - ABIN152503
Diaz, Christian, Anderson, McCool: Chronic ethanol and withdrawal differentially modulate lateral/basolateral amygdala paracapsular and local GABAergic synapses. in The Journal of pharmacology and experimental therapeutics 2011
Human Polyclonal GABARAP Primary Antibody for EIA, IF - ABIN1449614
Newman, Scholefield, Kemp, Newman, McIver, Kamal, Wilkinson: TBK1 kinase addiction in lung cancer cells is mediated via autophagy of Tax1bp1/Ndp52 and non-canonical NF-κB signalling. in PLoS ONE 2012
KBTBD6 and KBTBD7 specifically bind to GABARAP proteins.GABARAP proteins mediate localized ubiquitylation of TIAM1 (show TIAM1 Antibodies) by CUL3 (show CUL3 Antibodies).
Data show that WAC (show WAC Antibodies) directly binds to GM130 (show GOLGA2 Antibodies) 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 Antibodies)-Ube2E3 (show UBE2E3 Antibodies) supports the role of Mulan (show MUL1 Antibodies) as an important regulator of mitophagy.
The FLCN (show FLCN Antibodies)-GABARAP association is modulated by the presence of either folliculin (show FLCN Antibodies)-interacting protein (FNIP)-1 (show FNIP1 Antibodies) or FNIP2 (show FNIP2 Antibodies) and further regulated by ULK1 (show ULK1 Antibodies).
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 Antibodies) regulates autophagosome-lysosome fusion through homotypic fusion and protein sorting complex and LC3 (show MAP1LC3A Antibodies)/GABARAP proteins.
GABARBP dramatically inhibited VEGF (show VEGFA Antibodies)-induced endothelial cell proliferation, migration, and tube formation, as well as VEGFR-2 (show KDR Antibodies) phosphorylation in vitro.
knockdown of LC3B (show MAP1LC3B Antibodies) but not GABARAPs resulted in significant accumulation of p62/Sqstm1 (show SQSTM1 Antibodies), one of the selective substrates for autophagy
These results support the regulatory role of Bcl-2 (show BCL2 Antibodies) 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 Antibodies) expression.
DLG4/PSD95 (show DLG4 Antibodies) and GABARAP were analyzed using zebrafish embryos with morpholino knockdown system as a model organism.
Ablation of GABARAP inhibits tumor initiation and progression through enhancement of both antitumor immunity and cell death signaling.
Lipidation of the LC3 (show MAP1LC3A Antibodies)/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3 (show ATG3 Antibodies).
Results indicate that, compared with LC3 (show MAP1LC3A Antibodies), GABARAP is enriched in the axonal initial segments (AIS (show AR Antibodies)).
Gabarap functions in the immune system. It is involved in mitochondrial quality control in macrophages, and thus it influences Nlrp3 (show NLRP3 Antibodies) inflammasome-dependent inflammatory responses.
ATG8 (show MAP1LC3B Antibodies)-like proteins (MAP1LC3B (show MAP1LC3B Antibodies), GABARAP and GABARAPL1 (show GABARAPL1 Antibodies)) are novel interactors of MAPK15/ERK8 (show MAPK15 Antibodies), a MAP kinase (show MAPK1 Antibodies) 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 Antibodies) 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 Antibodies) is up-regulation and intestinal NaPi-IIb (show SLC34A2 Antibodies) 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 Antibodies) kinase-signaling pathway.
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