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SNCAIP encodes a protein containing several protein-protein interaction domains, including ankyrin-like repeats, a coiled-coil domain, and an ATP/GTP-binding motif. Additionally we are shipping SNCAIP Proteins (6) and SNCAIP Kits (2) and many more products for this protein.
Showing 10 out of 60 products:
Human Polyclonal SNCAIP Primary Antibody for IF, IHC (p) - ABIN2476664
Büttner, Delay, Franssens, Bammens, Ruli, Zaunschirm, de Oliveira, Outeiro, Madeo, Buée, Galas, Winderickx: Synphilin-1 enhances ?-synuclein aggregation in yeast and contributes to cellular stress and cell death in a Sir2-dependent manner. in PLoS ONE 2010
Differential expression of synphilin-1 isoforms (and alpha-synuclein and parkin (show PARK2 Antibodies)) was found in multiple system atrophy brains compared to control brain.
Synphilin-1 binds ATP, but not CTP (show CDS1 Antibodies).
Overexpression of human synphilin-1 in mice resulted in hyperphagia and obesity.
Overexpression of SP1 (show PSG1 Antibodies) in neurons, but not peripheral cells, increased the body weight of flies compared with that of non-transgenic controls. SP1 (show PSG1 Antibodies) increased food intake but did not affect locomotor activity
Although serine-129 phosphorylation of alpha-synuclein facilitates tubulin polymerization promoting protein (TPPP (show Tppp Antibodies))-mediated alpha-SYN oligomerization, this modification does not seem to play an inevitable role in the early step of alpha-SYN oligomer formation.
Mutation screening of SNCAIP identifies novel sequence variants using a bioinformatic approach; further studies are necessary to determine their possible functional consequences in South African patients with Parkinson's disease.
Neuronal survival factor MEF2D is decreased in human and experimental Parkinson's disease, a decrease that is specifically associated with alpha-synuclein accumulation and aggregation.
Synphilin-1 inhibits alpha-synuclein degradation by the proteasome.
Knockdown of Herp (show HERPUD1 Antibodies) gene unexpectedly facilitated the degradation of synphilin-1, and improved cell viability during proteasomal inhibition.
Data show that periphilin (show PPHLN1 Antibodies) displays an overlapping expression pattern with synphilin-1 in cellular and animal models and in Lewy bodies of Parkinson's disease (PD) patients, and support involvement of periphilin (show PPHLN1 Antibodies) in PD.
This study shows that alpha-synuclein is present in cerebellar glutamatergic terminals.
These results suggest that increased levels of NUB1 play a potential role in degradation of detergent-insoluble alpha-synuclein in vivo, although it is insufficient to degrade abnormal alpha-synuclein in Lewy body disease model mice.
SP1 (show SP1 Antibodies) results in a CCK (show CCK Antibodies) response deficiency that may contribute to the increased meal size and overall hyperphagia in synphillin-1 transgenic mice
TEM analysis of protein:inhibitor assays demonstrated that scyllo-inositol inhibits the aggregation of alpha-synuclein, suggesting the therapeutic potential of the small molecule in PD.
We exploited atomic force microscopy (AFM) for the selective, nanoscale confinement of alpha-Synuclein on gold to study the early stages of alpha-Synuclein aggregation and the effect of small molecules, like dopamine, on the aggregation process.
Sncaip physically interacts with PPP1 and affects PPP1 sorting to subcellular compartments.
Studies identify a novel function of synphilin-1 in controlling food intake and body weight, and may provide a unique obesity model for future studies of obesity pathogenesis and therapeutics.
Synphilin-1 can diminish the severity of alpha-synucleinopathy and play a neuroprotective role against A53T alpha-synuclein toxicity in vivo.
synphilin-1 has a role in skill learning and motor performance
expression of synphilin-1 shortens N1E-115 cell division doubling time, promotes neurite outgrowth, and protects against Rotenone-induced toxicity; synphilin-1 displays a neurotrophic effect in vitro, may play a neuroprotective role in Parkinson's disease
This gene encodes a protein containing several protein-protein interaction domains, including ankyrin-like repeats, a coiled-coil domain, and an ATP/GTP-binding motif. The encoded protein interacts with alpha-synuclein in neuronal tissue and may play a role in the formation of cytoplasmic inclusions and neurodegeneration. A mutation in this gene has been associated with Parkinson's disease. Alternatively spliced transcript variants encoding different isoforms of this gene have been described, but the full-length nature of only two have been determined.
synuclein, alpha interacting protein
, synuclein, alpha interacting protein (synphilin)
, alpha-synuclein-interacting protein
, synuclein alpha interacting protein
, synphilin-1 variant 1e