Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1), A53T Mutant Protein

Name: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1), A53T Mutant Protein
Brand: Novus Biologicals
SKU: NBP3-14767

Novus Biologicals, part of Bio-Techne | Catalog # NBP3-14767

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Product Specifications
Scientific Data
Preparation & Storage
Background
Product Documents
Specific Notices

Key Product Details

Conjugate

Unconjugated

Applications

Microscopy, Functional Assay, SDS-PAGE, Western Blot

View all alpha-Synuclein Proteins and Enzymes »

Product Specifications

Description

A full length recombinant protein of Human alpha-Synuclein

Source: E. coli

Uniprot ID: P37840

Amino Acid Sequence: MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA

Purity

>95%, by SDS-PAGE

Activity

100 uM A53T alpha-Synuclein protein monomer seeded with 10 uM A53T alpha-Synuclein protein pre-formed fibrils in 25 uM Thioflavin T (PBS pH 7.4, 100 ul reaction volume) generated a fluorescence intensity of 28 000 RFU after incubation at 37C with shaking at 600 rpm for 56 hours. Fluorescence measured by excitation at 450 nm and emission at 485 nm on a microplate reader.

Localization

Cytoplasm, Membrane, Nucleus

Protein / Peptide Type

Recombinant Protein

Scientific Data Images

In vitro assay: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1), A53T Mutant Protein [NBP3-14767]

In vitro assay: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1), A53T Mutant Protein [NBP3-14767] - 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 . A much greater increase in fluorescence is seen when 100 uM monomer is combined with 10 uM of fibrils (NBP3-14767) as the fibrils seed the formation of new fibrils from the pool of active monomers. Thioflavin T ex = 450 nm, em = 485 nm.

Electron Microscopy: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1), A53T Mutant Protein [NBP3-14767] - TEM of A53T alpha synuclein Pre-formed Fibrils (NBP3-14767)

Formulation, Preparation and Storage

NBP3-14767

Preparation Method	Ion-exchange Purified
Formulation	PBS pH 7.4
Preservative	No Preservative
Concentration	Please see the vial label for concentration. If unlisted please contact technical services.
Shipping	The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage	Store at -80C. Avoid freeze-thaw cycles.

Background: alpha-Synuclein

Alpha-synuclein, a member of the synuclein family, is a protein that was first identified in 1988 whose name is derived from its localization to both the synapse and nucleus (1-3). Specifically, it is expressed primarily in the brain, including Lewy Bodies (1-6). Alpha-synuclein is encoded by the SNCA gene, located on chromosome 4p21, and is processed as a 140 amino acid (aa) protein with a theoretical molecular weight of 14 kDa (1,2,4). Structurally alpha-synuclein consists of a N-terminal binding domain (1-60 aa), a central domain core region called the non-amyloid-beta component (NAC) (61-95 aa), and a C-terminal domain (96-140 aa) (1-3). The N-terminal region contains aa repeats with a KTKEGV consensus sequence that gives the protein its alpha-helical structure that associates with lipid membranes (1-4). The hydrophobic NAC region is responsible for alpha-synuclein aggregation and fibril formation (1-4). The acidic C-terminal tail is largely unstructured but can be targeted for post-translational modifications (1-4). The function of alpha-synuclein is not entirely understood, but it is shown to have a role in suppression of apoptosis, acting as a molecular chaperone, regulating glucose, and modulating calmodulin activity (1,3).

A number of studies have revealed that alpha-synuclein aggregation is a hallmark feature in a number of neurodegenerative diseases, referred to as synucleinopathies (2-4). Alpha-synuclein protein aggregates are a large component of Lewy bodies that are present in Parkinson's disease (PD), Lewy body dementia (LBD), and multiple system atrophy (1-6). Research has shown phosphorylation of alpha-synuclein at Ser129 moves the protein from the nucleus to the cytoplasm and promotes fibril formation associated with synucleinopathies (1,2,5). Recent studies also suggest that alpha-synuclein accumulation can prevent mitochondrial import machinery causing mitochondrial dysfunction that is often observed in neurodegeneration (5). It is thought that preventing alpha-synuclein aggregation may prevent PD, thus alpha-synuclein is a target for many potential therapeutic interventions aimed at decreasing aggregate formation or increasing clearance (1,2,4-6).

References

1. Villar-Pique, A., Lopes da Fonseca, T., & Outeiro, T. F. (2016). Structure, function and toxicity of alpha-synuclein: the Bermuda triangle in synucleinopathies. Journal of neurochemistry. https://doi.org/10.1111/jnc.13249

2. Emamzadeh F. N. (2016). Alpha-synuclein structure, functions, and interactions. Journal of research in medical sciences : the official journal of Isfahan University of Medical Sciences. https://doi.org/10.4103/1735-1995.181989

3. Burre J. (2015). The Synaptic Function of alpha-Synuclein. Journal of Parkinson's disease. https://doi.org/10.3233/JPD-150642

4. Lashuel, H. A., Overk, C. R., Oueslati, A., & Masliah, E. (2013). The many faces of alpha-synuclein: from structure and toxicity to therapeutic target. Nature reviews. Neuroscience. https://doi.org/10.1038/nrn3406

5. Rocha, E. M., De Miranda, B., & Sanders, L. H. (2018). Alpha-synuclein: Pathology, mitochondrial dysfunction and neuroinflammation in Parkinson's disease. Neurobiology of disease. https://doi.org/10.1016/j.nbd.2017.04.004

6. O'Leary, E. I., & Lee, J. C. (2019). Interplay between alpha-synuclein amyloid formation and membrane structure. Biochimica et biophysica acta. Proteins and proteomics. https://doi.org/10.1016/j.bbapap.2018.09.012

Alternate Names

NACP, PARK1, PARK4, SNCA, Synuclein-alpha

Gene Symbol

SNCA

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Product Specific Notices

Please note that the 200ug and 500ug sizes are sent in 2x100ug and 5x100ug vials, respectively

This product is for research use only and is not approved for use in humans or in clinical diagnosis. This product is guaranteed for 1 year from date of receipt.

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