Key features and details
- Mouse monoclonal [syn204] to Alpha-synuclein
- Suitable for: ICC
- Knockout validated
- Reacts with: Human
- Isotype: IgG2a
製品名Anti-Alpha-synuclein antibody [syn204]
Alpha-synuclein 一次抗体 製品一覧
製品の詳細Mouse monoclonal [syn204] to Alpha-synuclein
特異性Due to sequence homology ab3309 might react with Beta synuclein
アプリケーション適用あり: ICCmore details
Recombinant full length protein corresponding to Human Alpha-synuclein.
Database link: P37840
- ICC: HAP1 cells.
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保存方法Shipped at 4°C. Store at +4°C short term (1-2 weeks). Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Preservative: 0.1% Sodium azide
Concentration information loading...
精製度Protein G purified
The Abpromise guarantee
Use a concentration of 10 µg/ml.
Use a concentration of 10 µg/ml.
機能May 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.
組織特異性Expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals.
関連疾患Genetic 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
配列類似性Belongs to the synuclein family.
ドメインThe '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.
翻訳後修飾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.
細胞内局在Cytoplasm, cytosol. Membrane. Nucleus. Cell junction, synapse. Secreted. Membrane-bound in dopaminergic neurons.
- Information by UniProt
- Alpha synuclein antibody
- Alpha-synuclein antibody
- Alpha-synuclein, isoform NACP140 antibody
ab3309 staining Alpha-Synuclein in wild-type Hap1 cells (top panel) and SNCA knockout Hap1 cells (bottom panel). The cells were fixed with 4% paraformaldehyde (10 min) then permeabilized with 0.1% Triton X-100 for 5 minutes and then blocked with 1% BSA/10% normal goat serum/0.3M glycine in 0.1% PBS-Tween for 1h. The cells were then incubated with ab3309 at 10μg/ml concentration and ab6046 (Rabbit polyclonal to beta Tubulin) at 1/1000 dilution overnight at 4°C followed by a further incubation at room temperature for 1h with a goat secondary antibody to mouse IgG (Alexa Fluor® 488) (ab150117) at 2 μg/ml (shown in green) and a goat secondary antibody to rabbit IgG (Alexa Fluor® 594) (ab150080) at 2 μg/ml (shown in red). Nuclear DNA was labelled in blue with DAPI.
Image was taken with a confocal microscope (Leica-Microsystems TCS SP8).
ab3309 は 8 報の論文で使用されています。
- Park HJ et al. Ethanol extract from Gynostemma pentaphyllum ameliorates dopaminergic neuronal cell death in transgenic mice expressing mutant A53T human alpha-synuclein. Neural Regen Res 15:361-368 (2020). PubMed: 31552910
- Agerschou ED et al. An engineered monomer binding-protein for a-synuclein efficiently inhibits the proliferation of amyloid fibrils. Elife 8:N/A (2019). PubMed: 31389332
- Nevzglyadova OV et al. Yeast red pigment modifies cloned human a-synuclein pathogenesis in Parkinson disease models in Saccharomyces cerevisiae and Drosophila melanogaster. Neurochem Int 120:172-181 (2018). PubMed: 30099122
- Ma L et al. C-terminal truncation exacerbates the aggregation and cytotoxicity of a-Synuclein: A vicious cycle in Parkinson's disease. Biochim Biophys Acta Mol Basis Dis 1864:3714-3725 (2018). PubMed: 30290273
- Shahnawaz M et al. Development of a Biochemical Diagnosis of Parkinson Disease by Detection of a-Synuclein Misfolded Aggregates in Cerebrospinal Fluid. JAMA Neurol 74:163-172 (2017). PubMed: 27918765
- 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 . 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). PubMed: 25122523
- Croisier E et al. Comparative study of commercially available anti-alpha-synuclein antibodies. Neuropathol Appl Neurobiol 32:351-6 (2006). PubMed: 16640654