Recombinant human Alpha-synuclein (mutated A53T) protein monomer Type 1 (Active) (ab256149)
Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Active: Yes
- Suitable for: Functional Studies, SDS-PAGE
Description
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Product name
Recombinant human Alpha-synuclein (mutated A53T) protein monomer Type 1 (Active)
See all Alpha-synuclein proteins and peptides -
Biological activity
100 µM ab256149 seeded with 10 nM ab256150 in 25 µM Thioflavin T (PBS pH 7.4, 100 µl reaction volume) generated a fluorescence intensity of 28 000 Relative Fluorescence Units after incubation at 37°C with shaking at 600 rpm for 56 hours. Fluorescence was measured by excitation at 450 nm and emission at 485 nm on a Molecular Devices Gemini XPS microplate reader.
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Purity
> 95 % SDS-PAGE.
Purified by ion-exchange chromatography. -
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
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVH GVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQL GKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA -
Predicted molecular weight
14 kDa -
Amino acids
1 to 140 -
Modifications
mutated A53T -
Additional sequence information
NP_000336.1
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Description
Recombinant human Alpha-synuclein (mutated A53T) protein (Active)
Specifications
Our Abpromise guarantee covers the use of ab256149 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
SDS-PAGE
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Form
Liquid -
Additional notes
Monomer.
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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.
pH: 7.40
Constituent: 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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Thioflavin T is a fluorescent dye that binds to beta sheet-rich structures such as those in alpha synuclein fibrils. Upon binding, the emission spectrum of the dye experiences a red-shift and increased fluorescence intensity. Thioflavin T emission curves show a limited increase in fluorescence (correlated to alpha synuclein aggregation) over time in A53T alpha synuclein monomers (ab256149). A much greater increase in fluorescence is seen when 100 µM monomer (ab256149) is combined with 10 µM of fibrils (ab256150) as the fibrils seed the formation of new fibrils from the pool of active monomers. Thioflavin T ex = 450 nm, em = 485 nm.
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SDS-PAGE - Recombinant Alpha-Synuclein Monomer (mutated A53T) protein (ab256149).
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 (0)
ab256149 has not yet been referenced specifically in any publications.