SNCA (1-140) Antibody
Description
Antibody Characteristics
SNCA (1-140) antibodies are typically monoclonal or polyclonal reagents designed for diverse experimental applications. Key features include:
Neurodegenerative Disease Studies
SNCA (1-140) antibodies are pivotal in detecting pathological α-synuclein aggregates in PD and related synucleinopathies. Studies using these antibodies have revealed:
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Lewy Body Detection: α-Synuclein fibrils in Lewy bodies are a hallmark of PD, identifiable via IHC and IF .
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Post-Translational Modifications: Phosphorylation at Ser129 (common in PD) and truncations (e.g., residues 108–140) are detectable with epitope-specific variants .
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Mechanistic Insights: These antibodies validate α-synuclein’s role in synaptic vesicle regulation and dopamine transporter interactions .
Experimental Validation
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Western Blot: Detects monomeric (14–18 kDa) and oligomeric α-synuclein in brain lysates .
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ELISA: Quantifies α-synuclein levels in cerebrospinal fluid (CSF) or plasma, aiding biomarker research .
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Epitope Mapping: Antibodies like LASH-EGT403 (residues 1–5) and 5B10-A12 (residues 1–10) distinguish structural isoforms .
Clinical and Therapeutic Relevance
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Diagnostic Utility: Elevated α-synuclein levels in CSF correlate with PD progression, measurable via SNCA (1-140) ELISA .
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Therapeutic Development: Antibodies targeting residues 1–140 are used to evaluate anti-aggregation therapies in preclinical models .
Key Research Findings
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Pathogenic Aggregation: SNCA (1-140) antibodies confirm that familial PD mutations (e.g., A30P, A53T) accelerate α-synuclein fibrillization .
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Chaperone Activity Loss: Truncation of the C-terminal acidic tail (residues 96–140) abolishes α-synuclein’s chaperone function, a critical factor in neurodegeneration .
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Immune Response: Autoantibodies against α-synuclein (1-140) are detected in asymptomatic LRRK2 mutation carriers, suggesting early immune activation in PD .
Challenges and Considerations
Product Specs
SNCA antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
Product Science Overview
Alpha-synuclein is a protein predominantly expressed in the central nervous system, particularly in the neocortex, hippocampus, substantia nigra, thalamus, and cerebellum. It is primarily a neuronal protein but can also be found in neuroglial cells . The human alpha-synuclein protein consists of 140 amino acids and is encoded by the SNCA gene .
Alpha-synuclein is an intrinsically disordered protein, meaning it lacks a stable secondary or tertiary structure in solution. However, it can adopt partial alpha-helical and beta-sheet structures, as well as mostly structured tetrameric states . The protein is divided into three distinct domains:
- N-terminal region (1-60 a.a.): This region is amphipathic and dominated by four 11-residue repeats, including the consensus sequence KTKEGV, which has a structural alpha helix propensity similar to apolipoproteins-binding domains .
- Central hydrophobic region (61-95 a.a.): This region includes the non-amyloid-β component (NAC) region, which is involved in protein aggregation .
- C-terminal region (96-140 a.a.): This region is highly acidic and proline-rich .
Alpha-synuclein is involved in the regulation of dopamine release and transport and may function to induce fibrillization of microtubule-associated protein tau . It also acts as a molecular chaperone in the formation of SNARE complexes .
The mouse anti-human alpha-synuclein antibody is a monoclonal antibody that specifically targets the alpha-synuclein protein. It is used in various research applications, including immunohistochemistry and Western blotting . This antibody is produced by immunizing mice with a synthetic peptide corresponding to the carboxy-terminal sequence of human alpha-synuclein .
The mouse anti-human alpha-synuclein antibody is widely used in research to study the role of alpha-synuclein in neurodegenerative diseases, particularly Parkinson’s disease. It is also used to investigate the protein’s interactions with other cellular components and its involvement in synaptic transmission and membrane trafficking .
