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

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Western Blot: Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein [NBP2-54789] - Lane 1: Molecular Weight Ladder (MW). Lane 2: Active Alpha Synuclein Protein Aggregate.

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Summary
Reactivity HuSpecies Glossary
Applications WB, Func, ICC/IF, IHC, MS, PAGE, Bioactivity, NULL

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

Description
An un-tagged full length Human biologically active Alpha-Synuclein recombinant protein aggregate (pre-formed fibrils, Type 1), NCBI Accession #: NP_000336.1.

Source: E. coli

Amino Acid Sequence:

MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA
Details of Functionality
Endogenous alpha-synuclein phosphorylation. 100 uM alpha synuclein protein monomer (NBP2-54788) seeded with 10 uM alpha synuclein protein PFF (NBP2-54789) in 25 uM Thioflavin T (PBS pH 7.4, 100 ul reaction volume) generated a fluorescence intensity of 13,000 Relative Fluorescence Units after incubation at 37 degrees 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.
Source
E. coli
Protein/Peptide Type
Recombinant Protein
Gene
SNCA
Purity
Ion exchange chromatography

Applications/Dilutions

Dilutions
  • Bioactivity
  • Electron Microscopy
  • Immunocytochemistry/ Immunofluorescence
  • Immunohistochemistry
  • In vitro assay
  • In vivo assay
  • Product Image
  • SDS-Page 1:100-1:2000
  • Western Blot 1:100-1:2000
Theoretical MW
14.46 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

Storage
Store at -80C. Avoid freeze-thaw cycles.
Buffer
PBS
Purity
Ion exchange chromatography

Alternate Names for Recombinant Human alpha-Synuclein Active, Pre-formed Fibrils, (Type 1) Protein

  • alpha-Synuclein
  • I+/--synuclein
  • MGC110988
  • NACP
  • non A-beta component of AD amyloid
  • Non-A beta component of AD amyloid
  • Non-A4 component of amyloid precursor
  • PARK1
  • PARK4
  • PD1
  • SNCA
  • synuclein alpha-140
  • synuclein, alpha (non A4 component of amyloid precursor)
  • Synuclein-alpha
  • truncated alpha synuclein

Background

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

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

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Bioinformatics

Gene Symbol SNCA