Alpha Synuclein Oligomers

SKU:BHP11901186
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
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.
Options selector
Catalog no. Size
SPR-469B 100 ug
SPR-469C 100 ug x 2
SPR-469E 100 ug x 5
Field Specification
Accession Number NP_000336.1
Alternative Names Alpha synuclein protein, Alpha-synuclein oligomer, Alpha synuclein protein oligomer, Alpha-synuclein protein, Non-A beta component of AD amyloid protein, Non-A4 component of amyloid precursor protein, NACP protein, SNCA protein, NACP protein, PARK1 protein, Alpha synuclein oligomers, Alpha Synuclein Protein Oligomers, SYN protein, Parkinson's disease familial 1 Protein
Cellular Localization Cytoplasm | Membrane | Nucleus
Concentration 2 mg/ml
Conjugate
  • No Tag
Expression System
  • E. coli
Gene ID 6622
Product Type
  • Proteins & Peptide
  • Recombinant Protein
  • Chaperone & Stress Protein
Protein Length Full length
Protein Size ~14.46 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; native localization: Cytoplasm | Membrane | Nucleus).

Human Recombinant Alpha Synuclein Oligomers (Epigallocatechin gallate (EGCG) Stabilized)

Alpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimers disease amyloid plaque, and a major component of Lewy body inclusions, and Parkinson's disease. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin (5, 6). Epigallocatechin Gallate (EGCG) reduces alpha synuclein fibril formation in favour of spherical soluble oligomers (7).

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
  • Cellular localization (native): Cytoplasm | Membrane | Nucleus
  • Protein length: Full length
  • Protein size: ~14.46 kDa
  • Purity: >95%
  • Expression system: E. coli
  • Purification: Ion-exchange Purified
  • Storage buffer: PBS pH 7.4

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: Monomer source is catalog# SPR-316.

Certificate of Analysis: Certified >95% pure using SDS-PAGE analysis. Low endotoxin <5 EU/mL @ 2mg/mL.

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 Oligomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-469B)
Human Recombinant Alpha Synuclein Oligomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-469C)
Human Recombinant Alpha Synuclein Oligomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-469E)

What is the purity of Alpha Synuclein Oligomers (Human)?
>95% BioHippo includes a Certificate of Analysis (CoA) confirming purity per lot with every order.
How should Alpha Synuclein Oligomers (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. “Genetics Home Reference: SNCA”. US National Library of Medicine. (2013).
2. Zhang L., et al. (2008) Brain Res. 1244: 40-52.
3. Alim M.A., et al. (2002) J Biol Chem. 277(3): 2112-2117.
4. Kokhan V.S., Afanasyeva M.A., Van'kin G. (2012) Behav. Brain. Res. 231(1): 226-230.
5. Spillantini M.G., et al. (1997) Nature. 388(6645): 839-840.
6. Mezey E., et al. (1998) Nat Med. 4(7): 755-757.
7. Ehrnhoefer, D. E. et al. (2008). Nat Struct Mol Biol. 15(6):558-566.

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