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Rat (Rattus) SNCA Protein expressed in Rabbit - ABIN1742284
Jüttner, Moré, Das, Babich, Meier, Henning, Erdmann, Mu Ller, Otto, Grantyn, Rathjen: Impaired synapse function during postnatal development in the absence of CALEB, an EGF-like protein processed by neuronal activity. in Neuron 2005
Human SNCA Protein expressed in Escherichia coli (E. coli) - ABIN2005039
Lee, Choi, Lee: Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form. in The Journal of biological chemistry 2002
Show all 2 Pubmed References
study examined the spatial and temporal expression patterns of three synuclein genes (snca, sncbb, sncg) during embryogenesis
C57BL/6J-OlaHsd mice, a substrain of C57BL/6J carrying mutated alpha-synuclein and multimerin-1 (zeige MMRN1 Proteine) genes, have an altered bone phenotype.
The findings of this study indicated a functional role of alpha-synuclein in early experimental autoimmune encephalomyelitis by increasing Th1 (zeige HAND1 Proteine) cell-mediated immune response.
These data show that neurodegenerative processes associated with lysosomal dysfunction may be presynaptically initiated by a concomitant reduction in alpha-synuclein and CSPalpha levels at nerve terminals.
Data suggest that endocytosis is the principal mechanism by which proteopathic alpha-synuclein aggregates are internalized in primary hippocampal neurons in culture; aggregates are rapidly trafficked along endosomal/lysosomal pathway, where most of the material remains for days as proposed in neurodegenerative synucleinopathies.
LRRK2 (zeige LRRK2 Proteine) negatively regulates the clearance of alphaSYN accompanied by down-regulation of the endocytosis pathway; LRRK2 (zeige LRRK2 Proteine) in microglia may function as the offending molecule responsible for neurodegeneration, in terms of down-regulation of alphaSYN clearance.
sideroflexin 3 (SFXN3 (zeige SFXN3 Proteine)) was found to be a mitochondrial protein (zeige COX6B2 Proteine) localized to the inner mitochondrial membrane.
The ability of monomeric alpha-synuclein to enhance ATP synthase efficiency under physiological conditions may be of importance when alpha-synuclein undergoes the misfolding and aggregation
Rab7 (zeige RAB7A Proteine) accumulated in GCase (zeige GBA Proteine) deficient cells, supporting the notion that lysosomal recycling is impaired. Since recombinant GCase (zeige GBA Proteine) can reverse ALR (zeige GFER Proteine) impairment, we anticipate that strategies to restore GCase (zeige GBA Proteine) activity in the brains of both sporadic patients with PD and those with GBA1 (zeige GBA Proteine) mutations will improve autophagy lysosomal pathway, preventing the accumulation of a-synuclein and spread of pathology.
Study showed that apoptosis is an important form of cellular degeneration in lipopolysaccharide (LPS (zeige TLR4 Proteine)-sensitized hypoxic-ischemic (HI) injury in the immature brain. Loss of PINK1 (zeige PINK1 Proteine) can protect the immature brain against cell apoptosis induced by LPS (zeige TLR4 Proteine)-sensitized HI injury. Moreover, alpha-Syn plays a neuroprotective role in LPS (zeige TLR4 Proteine)-sensitized HI brain damage in PINK1 (zeige PINK1 Proteine)-knockout neonatal mice
Genetic manipulation of sirtuin 2 levels in vitro and in vivo modulates the levels of alpha-synuclein acetylation, its aggregation, and autophagy.
Alteration of structure and aggregation of alpha-synuclein by familial Parkinson's disease associated mutations have been summarized. (Review)
Methylation of SNCA-intron1 region does not correlate with alpha-synuclein expression in Parkinson's disease samples.
Raising dopamine levels in mice expressing human mutant alpha-synuclein induced progressive nigrostriatal degeneration.
Mutant GBA proteins cause increases in alpha-synuclein levels, while an inhibition of GBA by alpha-synuclein has been also demonstrated in Gaucher disease patients with Parkinson disease. (Review)
RER1 (zeige RER1 Proteine) is a novel and potential important mediator of elevated alphaSyn levels
Results show that both alphaS and NFL (zeige NEFL Proteine) can be phosphorylated by CKII (zeige CSNK2A1 Proteine), PLK2 (zeige PLK2 Proteine) and PLK3 (zeige PLK3 Proteine), but Ser129 in alphaS is a preferential site for PLK2 (zeige PLK2 Proteine) and PLK3 (zeige PLK3 Proteine), demonstrating higher phosphorylation efficiency. Comparatively, CKII (zeige CSNK2A1 Proteine) preferentially phosphorylates Ser473 in NFL (zeige NEFL Proteine) and this site can be phosphorylated by PLK1, 2 and 3, but these enzymes prefer to modify other sites within NFL (zeige NEFL Proteine).
two morphologically different alpha-synuclein fibrils, one helical and the other ribbon-like, are shown to form together. Surprisingly, a widely used small molecule for probing aggregation reactions, thioflavin T (ThT), was found to tune the structural heterogeneity found in the fibrils.
results indicated that the dismal prognosis of patients with HBsAg+ may be related to the high rate of PD1 (zeige PDCD1 Proteine) expression. Thus, a targeted PD1 (zeige PDCD1 Proteine) treatment strategy may improve the prognosis of HBsAg+ DLBCL patients
PD-1 (zeige PDCD1 Proteine) in osteosarcoma patients mediated follicular helper T cells suppression.
Data show that cyclophilin 40 (CyP40) interacts with and dissolves amyloids forming proteins tau and alpha-synuclein aggregates.
analysis of membrane curvature sensing by amphipathic helices using alpha-synuclein and annexin B12 (zeige TNFAIP1 Proteine) [ANXB12]
Immunocytochemistry shows alpha synuclein localized to the Golgi apparatus and vesicles of bovine adrenal medullary chromaffin cells, consistent with its putative role in vesicular function within synapses.
Alpha-synuclein is a member of the synuclein family, which also includes beta- and gamma-synuclein. Synucleins are abundantly expressed in the brain and alpha- and beta-synuclein inhibit phospholipase D2 selectively. SNCA may serve to integrate presynaptic signaling and membrane trafficking. Defects in SNCA have been implicated in the pathogenesis of Parkinson disease. SNCA peptides are a major component of amyloid plaques in the brains of patients with Alzheimer's disease. Four alternatively spliced transcripts encoding two different isoforms have been identified for this gene.
, alpha SYN
, non-A beta component of AD amyloid
, non-A4 component of amyloid
, non A-beta component of AD amyloid
, synuclein alpha-140
, alpha synuclein