Anti-Alpha-synuclein antibody [syn204] (ab3309)
- Datasheet
- References (3)
- Protocols
Overview
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Product nameAnti-Alpha-synuclein antibody [syn204]
See all Alpha-synuclein primary antibodies -
DescriptionMouse monoclonal [syn204] to Alpha-synuclein
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Host speciesMouse
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SpecificityDue to sequence homology ab3309 might react with Beta synuclein
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Tested applicationsSuitable for: IP, ICC/IF, WBmore details
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Species reactivityReacts with: Human
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Immunogen
Recombinant full length protein (Human).
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Positive control
- Brain.
Properties
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FormLiquid
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Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Store at -20°C or -80°C. Avoid freeze / thaw cycle.
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Storage bufferpH: 7.40
Preservative: 0.1% Sodium azide
Constituent: PBS -
Concentration information loading... -
PurityProtein G purified
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ClonalityMonoclonal
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Clone numbersyn204
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IsotypeIgG2a
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Light chain typekappa
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Research areas
Associated products
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Compatible Secondaries
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Isotype control
Applications
Our Abpromise guarantee covers the use of ab3309 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
| Application | Abreviews | Notes |
|---|---|---|
| IP | Use at an assay dependent concentration. | |
| ICC/IF | Use at an assay dependent concentration. | |
| WB | 1/200. |
Target
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FunctionMay be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation.
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Tissue specificityExpressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals.
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Involvement in diseaseGenetic alterations of SNCA resulting in aberrant polymerization into fibrils, are associated with several neurodegenerative diseases (synucleinopathies). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer disease amyloid plaque, and a major component of Lewy body inclusions. They are also found within Lewy body (LB)-like intraneuronal inclusions, glial inclusions and axonal spheroids in neurodegeneration with brain iron accumulation type 1.
Parkinson disease 1
Parkinson disease 4
Dementia Lewy body -
Sequence similaritiesBelongs to the synuclein family.
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DomainThe 'non A-beta component of Alzheimer disease amyloid plaque' domain (NAC domain) is involved in fibrils formation. The middle hydrophobic region forms the core of the filaments. The C-terminus may regulate aggregation and determine the diameter of the filaments.
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Post-translational
modificationsPhosphorylated, 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. -
Cellular localizationCytoplasm, cytosol. Membrane. Nucleus. Cell junction, synapse. Secreted. Membrane-bound in dopaminergic neurons.
- Information by UniProt
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Database links
- Entrez Gene: 6622 Human
- Omim: 163890 Human
- SwissProt: P37840 Human
- Unigene: 21374 Human
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Alternative names
- Alpha synuclein antibody
- Alpha-synuclein antibody
- Alpha-synuclein, isoform NACP140 antibody
see all
Protocols
References
This product has been referenced in:
- Bassil F et al. Reducing C-terminal truncation mitigates synucleinopathy and neurodegeneration in a transgenic model of multiple system atrophy. Proc Natl Acad Sci U S A 113:9593-8 (2016). SDS-PAGE . Read more (PubMed: 27482103) »
- Volpicelli-Daley LA et al. Addition of exogenous a-synuclein preformed fibrils to primary neuronal cultures to seed recruitment of endogenous a-synuclein to Lewy body and Lewy neurite-like aggregates. Nat Protoc 9:2135-46 (2014). Read more (PubMed: 25122523) »
