Description
Product name
Recombinant Human Alpha-synuclein protein aggregate (Active)See all Alpha-synuclein proteins and peptidesBiological activity
Endogenous alpha-synuclein phosphorylation.
100 µM alpha synuclein protein monomer (ab218818) seeded with 10 µM alpha synuclein protein aggregate (ab218819) 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 microplate reader.
Purity
>95% SDS-PAGE.ab218819 was purified by ion-exchange.Expression system
Escherichia coliAccession
P37840Protein length
Full length proteinAnimal free
NoNature
RecombinantSpecies
HumanSequence
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEAPredicted molecular weight
14 kDaAmino acids
1 to 140Additional sequence information
(NP_000336.1) (GeneID 6622)
Description
Recombinant human Alpha-synuclein protein (Active)
Associated products
Related Products
- Thioflavin T, Fluorescent cell-permeable amyloid binding benzothiazole salt (ab120751)
- Anti-Alpha-synuclein antibody [MJFR1] (ab138501)
- Anti-Alpha-synuclein antibody [4D6] (ab1903)
- Recombinant Human Alpha-synuclein protein aggregate (Type 2) (ab218817)
- Recombinant Human Alpha-synuclein protein monomer (Active) (ab218818)
- Anti-Alpha-synuclein antibody [LB 509] (ab27766)
Specifications
Our Abpromise guarantee covers the use ofab218819in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
- Applications
Western blot
Functional Studies
SDS-PAGE
Form
LiquidAdditional notes
Learn more.
- Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Store at-80°C. Avoid freeze / thaw cycle.
Constituent: PBS
This product is an active protein and may elicit a biological response in vivo, handle with caution.
General Info
Alternative names
- Alpha synuclein
- Alpha-synuclein
- Alpha-synuclein, isoform NACP140
see allFunction
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 1Parkinson disease 4Dementia Lewy bodySequence 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-translationalmodifications
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.Cellular localization
Cytoplasm, cytosol. Membrane. Nucleus. Cell junction, synapse. Secreted. Membrane-bound in dopaminergic neurons.- Information by UniProt