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The Golgi complex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum. Zusätzlich bieten wir Ihnen Acyl-CoA Binding Domain Containing 3 Proteine (8) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 76 products:
Human Monoclonal Acbd3 Primary Antibody für IF, IHC (p) - ABIN566272
Rönnberg, Jääskeläinen, Blot, Parviainen, Vaheri, Renkonen, Bouloy, Plyusnin: Searching for cellular partners of hantaviral nonstructural protein NSs: Y2H screening of mouse cDNA library and analysis of cellular interactome. in PLoS ONE 2012
Human Monoclonal Acbd3 Primary Antibody für IF, ELISA - ABIN528687
Soupene, Rothschild, Kuypers, Dean: Eukaryotic protein recruitment into the Chlamydia inclusion: implications for survival and growth. in PLoS ONE 2012
Human Polyclonal Acbd3 Primary Antibody für ICC, IF - ABIN4277560
Téoulé, Brisac, Pelletier, Vidalain, Jégouic, Mirabelli, Bessaud, Combelas, Autret, Tangy, Delpeyroux, Blondel: The Golgi protein ACBD3, an interactor for poliovirus protein 3A, modulates poliovirus replication. in Journal of virology 2013
Results show that Aichi virus 3A protein activates the lipid kinase activity of PI4KIIIb,which activation is sensitized by the protein ACBD3. The interfaces between PI4KIIIbeta (zeige PI4KB Antikörper)-ACBD3 and ACBD3-3A were mapped with hydrogen-deuterium exchange mass spectrometry.
Kobuviral non-structural 3A proteins act as molecular harnesses to hijack the host ACBD3 protein.
The authors propose a model in which interaction between Salmonella enterica serovar Typhimurium SseF and SseG enables both proteins to bind ACBD3, thereby anchoring Salmonella-containing vacuoles at the Golgi network and facilitating bacterial replication.
these findings suggest that ACBD3 has prominent impacts on cellular NAD(+) metabolism via regulating PARP1 (zeige PARP1 Antikörper) activation-dependent auto-modification and thus cell metabolism and function.
Authors found that NS5A and PI4KB (zeige PI4KB Antikörper) competed for association of acyl-coenzyme A (zeige SOAT2 Antikörper) binding domain containing protein 3 (zeige HSPB3 Antikörper) (ACBD3), which inhibited hepatitis C virus replication.
Host ACBD3, PI4KIIIBETA (zeige PI4KB Antikörper) and Aichi virus proteins complexes enhances phosphatidylinositol 4-phosphate synthesis and is critical for viral replication.
ACBD3 mediates mHtt cytotoxicity via a Rhes (zeige RASD2 Antikörper)/mHtt/ACBD3 complex.
Authors found that the Golgi protein (zeige GOLPH3 Antikörper) acyl-coenzyme A binding domain-containing 3 (ACBD3), interacts with the 3A proteins of poliovaccine Sabintpe 2 and coxsackievirus A17 at viral RNA replication sites.
Using affinity purification-mass spectrometry, we identified the putative Rab33 GTPase (zeige RACGAP1 Antikörper)-activating proteins TBC1D22A (zeige TBC1D22A Antikörper) and TBC1D22B (zeige TBC1D22B Antikörper) as ACBD3-interacting factors.
ACBD3 plays an essential role in maintaining lipid homeostasis via regulating SREBP1 (zeige SREBF1 Antikörper)'s processing pathway and thus impacting cellular lipogenesis.
ACBP3 participates in plant response to hypoxia by modulating VLCFA metabolism.
Three cis (zeige CISH Antikörper)-responsive elements (Dof, GT-1 (zeige SLC2A1 Antikörper), and the S-box) in the 5'-flanking region of ACBP3 are proven functional in the regulation of ACBP3.
The enhanced pathogenesis-related gene expression and P. syringae DC3000 resistance in the ACBP3-overexpressors are dependent on the NPR1-mediated, but not the COI1-mediated, signaling pathway.
ACBP3 is an important regulator of the ATG8 (zeige GABARAPL2 Antikörper)- phosphatidylethanolamine (PE) complex via its interaction with PE.
Investigations on ACBP3 reported here show its upregulation upon dark treatment and in senescing rosettes.
Acyl-CoA (zeige GLYAT Antikörper)-binding protein3 (ACBP3) localizes extracellularly and the affinities of the acyl-CoA (zeige GLYAT Antikörper)-binding domain in ACBP3 are investigated by in vitro binding assays. [ACBP3]
These results suggest that PBR (zeige TSPO Antikörper), in addition to its role in cholesterol and coproporphyrinogen III transport, is also directing the mitochondrial PPIX import, a function that can be ascribed to the 18kDa (zeige SEC11A Antikörper) PBR (zeige TSPO Antikörper) protein alone
Study reports that ACBD3 is a Numb (zeige NUMB Antikörper) partner in cell-fate specification, ACBD3 and Numb (zeige NUMB Antikörper) proteins interact through an essential Numb (zeige NUMB Antikörper) domain, and the respective loss- and gain-of-function mutant mice share phenotypic similarities.
The Golgi complex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum. The protein encoded by this gene is involved in the maintenance of Golgi structure and function through its interaction with the integral membrane protein giantin. It may also be involved in the hormonal regulation of steroid formation.
Golgi resident protein GCP60
, acyl-Coenzyme A binding domain containing 3
, DMT1-associated protein
, acyl-CoA-binding domain-containing protein 3
, golgi complex-associated protein 1
, golgi phosphoprotein 1
, neurotrophin receptor alike death domain protein
, p75-like apoptosis-inducing death domain protein
, PBR- and PKA-associated protein 7
, PKA (RIalpha)-associated protein
, golgi complex associated protein 1, 60kDa
, peripheral benzodiazepine receptor-associated protein PAP7
, PBR associated protein
, golgi complex associated protein 1, 60 kDa
, peripherial benzodiazepine receptor associated protein