α-synuclein aggregate Antibody [C4F17]

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
IHC1:2000 IF1:5000

Application
IHC, IF

Reactivity
Mouse, Rat, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Positive Control	Mouse colon tissue; Rat dorsal root ganglian (DRG) tissue; Human DLB brain tissue; ReNcell VM cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
α-synuclein aggregate Antibody [C4F17] detects endogenous levels of total α-synuclein aggregate protein.

Clone
C4F17

Synonym(s)
NACP; PARK1; SNCA; Alpha-synuclein; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor

Background
α-Synuclein aggregates constitute the defining pathological hallmark of synucleinopathies including Parkinson's disease, Dementia with Lewy Bodies, and Multiple System Atrophy, forming through conformational conversion of natively unstructured 140-amino-acid presynaptic protein α-synuclein into toxic β-sheet-rich amyloid fibrils via nucleation-dependent polymerization accelerated by Ser129 phosphorylation and oxidative stress. Native α-synuclein contains N-terminal amphipathic KTKEGV repeats enabling α-helical membrane binding and vesicle association, central NAC region's hydrophobic core driving amyloidogenic β-strand conversion, and C-terminal acidic-proline-rich domain inhibiting premature aggregation, but pathological prefibrillar oligomers acquire pore-forming properties disrupting synaptic vesicle trafficking, impairing mitochondrial complex I activity with reactive oxygen species production and calcium dysregulation, compromising lysosomal/proteasomal clearance mechanisms, and triggering chronic microglial neuroinflammation through TLR2/4 signaling pathways. Monomeric α-synuclein chaperones SNARE complex assembly optimizing dopamine neurotransmission while maintaining synaptic vesicle pools, yet soluble oligomeric intermediates rather than mature fibrils represent primary neurotoxins mediating selective nigral dopaminergic degeneration via prion-like templated misfolding propagation across neural circuits, with SNCA gene triplications and mutations (A53T, A30P, E46K) dramatically accelerating aggregation kinetics in familial cases while sporadic synucleinopathies reflect acquired proteostasis collapse.

Background

α-Synuclein aggregates constitute the defining pathological hallmark of synucleinopathies including Parkinson's disease, Dementia with Lewy Bodies, and Multiple System Atrophy, forming through conformational conversion of natively unstructured 140-amino-acid presynaptic protein α-synuclein into toxic β-sheet-rich amyloid fibrils via nucleation-dependent polymerization accelerated by Ser129 phosphorylation and oxidative stress. Native α-synuclein contains N-terminal amphipathic KTKEGV repeats enabling α-helical membrane binding and vesicle association, central NAC region's hydrophobic core driving amyloidogenic β-strand conversion, and C-terminal acidic-proline-rich domain inhibiting premature aggregation, but pathological prefibrillar oligomers acquire pore-forming properties disrupting synaptic vesicle trafficking, impairing mitochondrial complex I activity with reactive oxygen species production and calcium dysregulation, compromising lysosomal/proteasomal clearance mechanisms, and triggering chronic microglial neuroinflammation through TLR2/4 signaling pathways. Monomeric α-synuclein chaperones SNARE complex assembly optimizing dopamine neurotransmission while maintaining synaptic vesicle pools, yet soluble oligomeric intermediates rather than mature fibrils represent primary neurotoxins mediating selective nigral dopaminergic degeneration via prion-like templated misfolding propagation across neural circuits, with SNCA gene triplications and mutations (A53T, A30P, E46K) dramatically accelerating aggregation kinetics in familial cases while sporadic synucleinopathies reflect acquired proteostasis collapse.

References
https://pubmed.ncbi.nlm.nih.gov/34733860/ https://pubmed.ncbi.nlm.nih.gov/35681426/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%