Recombinant Human Alpha-synuclein protein monomer (Active) (ab218818)
Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Active: Yes
- Suitable for: Functional Studies, WB, SDS-PAGE
Product nameRecombinant Human Alpha-synuclein protein monomer (Active)
See all Alpha-synuclein proteins and peptides
100 µM alpha synuclein protein monomer (ab218818), seeded with 10 µM alpha synuclein protein aggregate in 25 µM Thioflavin T (ab120751) (PBS pH 7.4, 100 µl reaction volume), generated a fluorescence intensity of 13,000 Relative Fluorescence Units after incubation at 37°C with shaking at 600 rpm for 24 hours.
Fluorescence was measured by excitation at 450 nm and emission at 485 nm, on a Molecular Devices Gemini XPS microplate reader.
Endotoxin Level: 10-20 EU/mL
Purity> 95 % SDS-PAGE.
ab218818 is purified by ion exchange.
Expression systemEscherichia coli
Protein lengthFull length protein
SequenceMDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA
Predicted molecular weight14 kDa
Amino acids1 to 140
Additional sequence information(NP_000336.1) (GeneID 6622)
DescriptionRecombinant human Alpha-synuclein protein (Active)
- Thioflavin T, Fluorescent cell-permeable amyloid binding benzothiazole salt (ab120751)
- Anti-Alpha-synuclein antibody [MJFR1] (ab138501)
- Anti-Alpha-synuclein antibody [4D6] - BSA and Azide free (ab1903)
- Recombinant Human Alpha-synuclein protein monomer (Type 2) (ab218816)
- Recombinant Human Alpha-synuclein protein aggregate (Active) (ab218819)
- Anti-Alpha-synuclein antibody [LB 509] (ab27766)
Our Abpromise guarantee covers the use of ab218818 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.
Constituent: 95% PBS
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Alpha synuclein
- Alpha-synuclein, isoform NACP140
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.
Tissue specificityExpressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals.
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.
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.
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
SDS-PAGE of ~14 kDa Human Recombinant Alpha Synuclein Protein Monomer (SPR-321). Lane 1: Molecular Weight Ladder (MW). Lane 2: Alpha Synuclein Protein Monomer (2 µg) (SPR-321).
ThT emission curves show increased fluorescence (correlated to alpha-synuclein protein aggregation) over time when 10 µM of active alpha-synuclein aggregate (ab218819) is combined with 100 µM of active alpha-synuclein monomer (ab218818) (light blue), as compared to when 100 µM of control alpha-synuclein monomer (ab218816) is combined with 10 µM of active alpha-synuclein aggregate (ab218819) (dark blue).
ThT ex = 450 nm, em = 485 nm. View protocol.
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
ab218818 has been referenced in 2 publications.
- Uçar B et al. Spreading of Aggregated α-Synuclein in Sagittal Organotypic Mouse Brain Slices. Biomolecules 12:N/A (2022). PubMed: 35204664
- Ho PW et al. Long-term inhibition of mutant LRRK2 hyper-kinase activity reduced mouse brain α-synuclein oligomers without adverse effects. NPJ Parkinsons Dis 8:115 (2022). PubMed: 36088364