Recombinant Mouse alpha-Synuclein Active, Monomer, (Type 1) Protein
Novus Biologicals | Catalog # NBP2-61595
Key Product Details
Source
Applications
Product Specifications
Description
Source: E. coli
Amino Acid Sequence:
MDVFMKGLSKAKEGVVAAAE KTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA
Purity
Predicted Molecular Mass
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.
Activity
Protein / Peptide Type
Scientific Data Images for Recombinant Mouse alpha-Synuclein Active, Monomer, (Type 1) Protein
In vitro assay: Recombinant Mouse alpha-Synuclein Active, Monomer, (Type 1) Protein [NBP2-61595]
In vitro assay: Recombinant Mouse alpha-Synuclein Active, Monomer, (Type 1) Protein [NBP2-61595] - Active alpha synuclein aggregate seeds the formation of new alpha Synuclein aggregates from the pool of active monomers. 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. Thioflavin T emission curves show increased fluorescence (correlated to alpha Synuclein protein aggregation) over time when 10 nM of active alpha Synuclein aggregate is combined with 100 uM of active alpha Synuclein monomer, as compared to active alpha Synuclein aggregate and active alpha Synuclein monomer alone. Thioflavin T excitation maximum = 450 nm; emission maximum = 485 nm.Formulation, Preparation, and Storage
NBP2-61595
| Formulation | PBS |
| 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 in the dark. Avoid freeze-thaw cycles. |
Background: alpha-Synuclein
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
Gene Symbol
Additional alpha-Synuclein Products
Product Documents for Recombinant Mouse alpha-Synuclein Active, Monomer, (Type 1) Protein
Certificate of Analysis
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Product Specific Notices for Recombinant Mouse alpha-Synuclein Active, Monomer, (Type 1) 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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Protocols
Find general support by application which include: protocols, troubleshooting, illustrated assays, videos and webinars.
- Cellular Response to Hypoxia Protocols
- R&D Systems Quality Control Western Blot Protocol
- Troubleshooting Guide: Western Blot Figures
- Western Blot Conditions
- Western Blot Protocol
- Western Blot Protocol for Cell Lysates
- Western Blot Troubleshooting
- Western Blot Troubleshooting Guide
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FAQs for Recombinant Mouse alpha-Synuclein Active, Monomer, (Type 1) Protein
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Q: I'm looking for an alpha-Synuclein antibody with an epitope located in the first half (N-terminus) of the protein - preferably a monoclonal antibody. Can you help me with that?
A: Please take a look at NB110-57475. It has been validated for human, rat and mouse and the applications ICC and WB and the epitope it detects is in the N terminal.