Recombinant Human alpha-Synuclein Active, Monomer, (Type 2) Protein

Name: Recombinant Human alpha-Synuclein Active, Monomer, (Type 2) Protein
Brand: Novus Biologicals
SKU: NBP2-54786

Novus Biologicals, part of Bio-Techne | Catalog # NBP2-54786

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

Key Product Details

Source

E. coli

Conjugate

Unconjugated

Applications

Bioactivity, Functional Assay, SDS-PAGE, Western Blot

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Product Specifications

Description

An un-tagged full length Human Recombinant Alpha Synuclein Protein Monomer, Accession #: NP_000336.1

Source: E. coli

Amino Acid Sequence:
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA

Purity

Ion exchange chromatography

Predicted Molecular Mass

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.

Application Notes

In vitro assay: Active alpha synuclein aggregate (NBP2-54789) seeds the formation of new alpha Synuclein aggregates from the pool of active alpha Synuclein monomers (NBP2-54788). Thioflavin T is a fluorescent dye that binds to beta sheet-rich structures, such as those in alpha Synuclein aggregates. Upon binding, the emission spectrum of the dye experiences a red-shift, and increased fluorescence intensity.

Protein / Peptide Type

Recombinant Protein

Scientific Data Images for Recombinant Human alpha-Synuclein Active, Monomer, (Type 2) Protein

In vitro assay: Recombinant Human alpha-Synuclein Active, Monomer, (Type 2) Protein [NBP2-54786]

In vitro assay: Recombinant Human alpha-Synuclein Active, Monomer, (Type 2) Protein [NBP2-54786] - 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

SDS-PAGE: Recombinant Human alpha-Synuclein Active, Monomer, (Type 2) Protein [NBP2-54786]

SDS-Page: Recombinant Human alpha-Synuclein Active, Monomer, (Type 2) Protein [NBP2-54786] - SDS-PAGE of ~14 kDa Human Recombinant alpha-Synuclein Protein Monomer (NBP2-54786). Lane 1: Molecular Weight Ladder (MW). Lane 2: BSA (2.5 g). Lane 3: BSA (5 g). Lane 4: alpha-Synuclein Protein Monomer (2.5 g) (NBP2-54786). Lane 5: alpha-Synuclein Protein Monomer (5 g) (NBP2-54786).

Formulation, Preparation and Storage

NBP2-54786

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 for Recombinant Human alpha-Synuclein Active, Monomer, (Type 2) Protein

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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