| Field | Specification |
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| Mfr No | |
| Alternative Names | SNCA, alpha-synuclein, synuclein, Alpha synuclein monomer, Alpha-synuclein monomer, Alpha synuclein protein monomer, Alpha synuclein monomer, Alpha-synuclein protein, SNCA protein |
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| Conjugate | |
| Expression System | |
| Product Type | |
| Protein Length | |
| Protein Size | |
| Purity | |
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Background
Alpha-synuclein is provided as a recombinant protein reagent for research use only. It is commonly used as a defined molecular component in biochemical and cell-free systems where controlled protein input supports mechanistic study and assay development.
Protein identity context: Alpha-synuclein (source species: Human).
Human Recombinant Alpha Synuclein A90C Mutant Monomers
Thioflavin-T (ThT) fluorescence remains a common measurement of alpha-synuclein fibril formation, yet ThT exhibits poor affinity for oligomers and early aggregates. The alpha-synuclein A90C mutant monomers can be specifically labelled with alternative fluorophores (such as Alexa 488/Alexa 647) via maleimide chemistry to enable more sensitive FRET analysis of aggregation. The A90C mutant showed no perturbation of monomer structure and Alexa Fluor dye attachment to cysteine 90 was demonstrated to have no effect on the kinetics of fibril formation (1-3). Residue 90 is at the periphery of the NAC region, a key constituent of the alpha-synuclein β-sheet fibril core, which results in fluorophores on different monomers coming into close proximity upon formation of β-sheet structure during aggregation (4).
Biological significance and function
Alpha-synuclein is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This protein is frequently discussed in research themes such as Neuroscience and Neurodegeneration.
Molecular characteristics
Molecular characteristics: Key molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent proteins.
- Source species: Human
- Protein length: Full length (1 - 140 aa)
- Protein size: 14.49 kDa
- Purity: >95%
- Expression system: E. coli
- Purification: Ion-exchange Purified
- Storage buffer: 20mM Hepes pH 7.4, 150mM NaCl, 1mM TCEP pH 7.0
Post-translational considerations: E. coli expression typically yields a non-glycosylated recombinant form. This is often appropriate for intracellular enzymes and many binding studies, but extracellular ligands/receptors or disulfide-rich proteins may show activity or stability differences when PTMs are required.
Expression and purification strategy
Expression system: E. coli. Expression host choice can influence folding and PTM state, which may affect binding or activity depending on protein class.
Purification strategy: Ion-exchange Purified. Purification method and formulation help determine sample homogeneity and background in downstream biochemical assays.
Research interpretation
Research interpretation: Recombinant protein reagents can support controlled experiments such as reconstitution of molecular interactions, quantitative calibration, and mechanistic perturbation studies with defined inputs. Interpreting outcomes typically benefits from pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex formation.
Other relevant information: TCEP present to prevent disulfide bonds. Maleimide coupling reactions can be performed efficiently in the presence of TCEP.
Certificate of Analysis: Protein certified >95% pure on SDS-PAGE & Nanodrop analysis
Tariff Code: 3822.19.0030
UNSPSC Code: 12352202
ADR Code: Non-hazardous
UN Code for transport: Non-hazardous
Cite this Product: Human Recombinant Alpha Synuclein A90C Mutant Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-478B)
Human Recombinant Alpha Synuclein A90C Mutant Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-478C)
Human Recombinant Alpha Synuclein A90C Mutant Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-478E)
What is the purity of Alpha Synuclein A90C Mutant Monomers (Human)?
How should Alpha Synuclein A90C Mutant Monomers (Human) be stored?
What expression system was used to produce this protein?
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Is this protein approved for clinical or in vitro diagnostic use?
Can I request a custom size, tag variant, or formulation?
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
2.Cremades, et al. 2012. Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein. Cell. 149(5): 1048-59. doi: 10.1016/j.cell.2012.03.037
3.Horrocks et al. 2015. Fast Flow Microfluidics and Single-Molecule Fluorescence for the Rapid Characterization of α-Synuclein Oligomers. Anal. Chem. 87(17): 8818-26. https://doi.org/10.1021/acs.analchem.5b01811
4.Iljina et al. 2016. Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading. PNAS. 113(19): E1206-15. doi: 10.1073/pnas.1524128113
5.Masuda, et al. 2006. Cysteine misincorporation in bacterially expressed human alpha-synuclein. FEBS Lett. 580(7): 1775-9. doi: 10.1016/j.febslet.2006.02.032