Alpha Synuclein A90C Mutant Monomers

SKU:BHP11901235
Overview
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Alpha-synuclein recombinant protein (Human) for research use. Supplied as a defined reagent (expressed in E. coli; purity >95%) to support controlled biochemical studies and assay development.
Target Alpha-synuclein
Species Human
Expression System E. coli
Conjugate No Tag
Purity >95%
Protein Length Full length (1 - 140 aa)
Options selector
Catalog no. Size
SPR-478B 100 ug
SPR-478C 100 ug x 2
SPR-478E 100 ug x 5
Available Options

Select from the available variant options shown for this product. Review lead time and shipping expectations before ordering.

  • Options: Size (100 ug, 100 ug x 2, 100 ug x 5).
  • Lead time: in-stock options typically ship in 2–3 business days.
  • Storage: store at -80°C; cold-chain shipment (typically with dry ice) is expected.
  • Please ensure someone is available to receive and store the shipment promptly.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No SPR-478
Alternative Names SNCA, alpha-synuclein, synuclein, Alpha synuclein monomer, Alpha-synuclein monomer, Alpha synuclein protein monomer, Alpha synuclein monomer, Alpha-synuclein protein, SNCA protein
Concentration 2 mg/ml
Conjugate
  • No Tag
Expression System
  • E. coli
Product Type
  • Proteins & Peptide
  • Recombinant Protein
  • Chaperone & Stress Protein
Protein Length Full length (1 - 140 aa)
Protein Size 14.49 kDa
Purity >95%
Shipping Dry Ice. Shipping note: Product will be shipped separately from other products purchased in the same order.
Species Human
Storage -80ºC
Target Alpha-synuclein

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)?
>95% BioHippo includes a Certificate of Analysis (CoA) confirming purity per lot with every order.
How should Alpha Synuclein A90C Mutant Monomers (Human) be stored?
-80ºC Prepare single-use aliquots after reconstitution to avoid repeated freeze–thaw cycles.
What expression system was used to produce this protein?
This recombinant protein was expressed in E. coli. The system was selected to achieve high yield, correct folding, and appropriate post-translational modifications.
What are the shipping conditions?
Dry Ice. Shipping note: Product will be shipped separately from other products purchased in the same order. Upon receipt, immediately transfer to recommended storage conditions.
Is this protein approved for clinical or in vitro diagnostic use?
No. Supplied for Research Use Only (RUO) — not intended for therapeutic applications or in vitro diagnostic procedures.
Can I request a custom size, tag variant, or formulation?
Yes. BioHippo can accommodate custom requests including alternative sizes, His/GST/Fc tag variants, bulk quantities, and custom formulations. See the Customization & Add-ons tab or email support@biohippo.com.

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.

1.Thirunavukkuarasu, et al. 2008. Multiparametric Flurorescence Detection of Early Stages in the Amylord Protein Aggregation of Pyrene-labeled α-Synuclein. J. Mol. Biol. 378(5): 1064-73. https://doi.org/10.1016/j.jmb.2008.03.034
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
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