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
Description
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Product name
Recombinant Human Alpha-synuclein protein monomer (Active)
See all Alpha-synuclein proteins and peptides -
Biological activity
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
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Purity
> 95 % SDS-PAGE.
ab218818 is purified by ion exchange. -
Expression system
Escherichia coli -
Accession
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Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA -
Predicted molecular weight
14 kDa -
Amino acids
1 to 140 -
Additional sequence information
(NP_000336.1) (GeneID 6622)
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Description
Recombinant human Alpha-synuclein protein (Active)
Associated products
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Related Products
- 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)
Specifications
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.
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Applications
Functional Studies
Western blot
SDS-PAGE
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Form
Liquid -
Additional notes
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.
pH: 7.40
Constituent: 95% PBSThis product is an active protein and may elicit a biological response in vivo, handle with caution.
General Info
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Alternative names
- Alpha synuclein
- Alpha-synuclein
- Alpha-synuclein, isoform NACP140
see all -
Function
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. -
Tissue specificity
Expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals. -
Involvement in disease
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 -
Sequence similarities
Belongs to the synuclein family. -
Domain
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. -
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 localization
Cytoplasm, cytosol. Membrane. Nucleus. Cell junction, synapse. Secreted. Membrane-bound in dopaminergic neurons. - Information by UniProt
Images
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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).
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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.
Protocols
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
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Datasheet download
References (2)
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