Recombinant mouse Alpha-synuclein protein Type 1 (Active) (ab256155)
Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Active: Yes
- Suitable for: SDS-PAGE, Functional Studies
Description
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Product name
Recombinant mouse Alpha-synuclein protein Type 1 (Active)
See all Alpha-synuclein proteins and peptides -
Biological activity
100µM Alpha-synuclein protein monomer (ab256155) seeded with 10nM alpha synuclein protein PFF (ab246002) in 25 µM Thioflavin T (PBS pH 7.4, 100 µl reaction volume) generated an increased fluorescence intensity 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.
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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
Mouse -
Sequence
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVH GVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQM GKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA -
Predicted molecular weight
14 kDa -
Amino acids
1 to 140
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Description
Recombinant mouse Alpha-synuclein protein (Active)
Specifications
Our Abpromise guarantee covers the use of ab256155 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
SDS-PAGE
Functional Studies
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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.
Constituent: PBS
This 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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Type 1 alpha synuclein preformed fibrils (ab246002) seed the formation of new alpha synuclein fibrils from the pool of alpha synuclein monomers (ab256155). 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 increased fluorescence (correlated to alpha synuclein protein aggregation) over time when 10 µM of Type 1 alpha synuclein preformed fibrils (ab246002) is combined with 100 µM of alpha synuclein monomer (ab256155), as compared to Type 1 alpha synuclein preformed fibrils (ab246002) or alpha synuclein monomer (ab256155) alone. Thioflavin T ex = 450 nm, em = 485 nm.
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SDS-PAGE - 2µg Mouse Recombinant Alpha-synuclein Protein Monomer (ab256155).
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)
ab256155 has not yet been referenced specifically in any publications.