| Weight | 1 lbs |
|---|---|
| Dimensions | 9 × 5 × 2 in |
| host | mouse |
| isotype | IgG1 |
| clonality | monoclonal |
| concentration | 1 mg/mL |
| applications | ICC/IF, IHC, WB |
| available sizes | 100 µg |
mouse anti-Alpha-synuclein monoclonal antibody (211) 9067
$409.00
Antibody summary
- Mouse monoclonal to Alpha-synuclein
- Suitable for: WB, ICC/IF, IHC
- Reacts with: human, mouse, rat
- Isotype: IgG1
- 100 µg
mouse anti-Alpha-synuclein monoclonal antibody (211) 9067
| target relevance |
|---|
| Alpha-synuclein is a crucial protein involved in synaptic function and neurotransmitter release, primarily found in presynaptic terminals of neurons. In research, alpha-synuclein has gained significant attention as a potential cell marker for neurodegenerative diseases, particularly Parkinson's disease. The aggregation of alpha-synuclein into insoluble fibrils is a hallmark of Parkinson's pathology, and its presence in Lewy bodies is a diagnostic feature of the disease. Therefore, alpha-synuclein is utilized as a marker to identify and study Parkinson's disease-related pathology in postmortem brain tissues and experimental models. Antibodies targeting alpha-synuclein are extensively employed in immunohistochemistry and western blotting to visualize and quantify its expression levels in various brain regions and cellular compartments. Click for more on: cell markers and alpha synuclein |
| Protein names Alpha-synuclein (Non-A beta component of AD amyloid) (Non-A4 component of amyloid precursor) (NACP) |
| Gene names SNCA,SNCA NACP PARK1 |
| Protein family Synuclein family |
| Mass 14460Da |
| Function Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (PubMed:28288128, PubMed:30404828, PubMed:20798282, PubMed:26442590). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (PubMed:28288128, PubMed:30404828). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (PubMed:30404828). Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (PubMed:20798282). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (PubMed:20798282). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (PubMed:26442590). |
| Subellular location Cytoplasm Membrane Nucleus Synapse Secreted Cell projection, axon Note=Membrane-bound in dopaminergic neurons (PubMed:15282274). Expressed and colocalized with SEPTIN4 in dopaminergic axon terminals, especially at the varicosities (By similarity). |
| Tissues Highly expressed in presynaptic terminals in the central nervous system. Expressed principally in brain. |
| Structure Soluble monomer. Homotetramer (PubMed:21841800). A dynamic intracellular population of tetramers and monomers coexists normally and the tetramer plays an essential role in maintaining homeostasis (PubMed:21841800). Interacts with UCHL1 (By similarity). Interacts with phospholipase D and histones. Interacts (via N-terminus) with synphilin-1/SNCAIP; this interaction promotes formation of SNCA inclusions in the cytoplasm (PubMed:19762560). Interacts with CALM1 (PubMed:23607618). Interacts with STXBP1; this interaction controls SNCA self-replicating aggregation (PubMed:27597756). Interacts with SNARE components VAMP2 and SNAP25; these interactions allows SNARE complex assembly and integrity (PubMed:20798282). Interacts with RPH3A and RAB3A (PubMed:15207266). Interacts with SERF1A; this interaction promotes the aggregation of SNCA (PubMed:22854022, PubMed:31034892). Interacts with SEPTIN4 (By similarity). |
| Post-translational modification Phosphorylated, predominantly on serine residues. Phosphorylation by CK1 appears to occur on residues distinct from the residue phosphorylated by other kinases. Phosphorylation of Ser-129 is selective and extensive in synucleinopathy lesions. In vitro, phosphorylation at Ser-129 promoted insoluble fibril formation. Phosphorylated on Tyr-125 by a PTK2B-dependent pathway upon osmotic stress. ; Hallmark lesions of neurodegenerative synucleinopathies contain alpha-synuclein that is modified by nitration of tyrosine residues and possibly by dityrosine cross-linking to generated stable oligomers.; Ubiquitinated. The predominant conjugate is the diubiquitinated form. ; Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure. |
| Target Relevance information above includes information from UniProt accession : P37840 |
| The UniProt Consortium |
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Publications
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.| pmid | title | authors | citation |
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Protocols
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| Western blot IHC ICC |
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