| Field | Specification |
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| Mfr No | |
| Alternative Names | Alpha synuclein, Alpha-synuclein pre-formed fibril, Alpha synuclein protein PFF, Alpha synuclein PFF, 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, SYN protein, Parkinson disease familial 1 Protein |
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| Conjugate | |
| Expression System | |
| Product Type | |
| Protein Length | |
| Protein Size | |
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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 pSer129 PFFs (phosphorylated at position 129)
Serine 129 is the C-terminal serine characteristic to mammalian alpha synuclein, with this serine being determined to be a major phosphorylation site (1). Lewy Bodies in Parkinson’s Disease (PD) and other related synucleinopathies are comprised of alpha synuclein phosphorylated at serine 129 and this phosphorylation may contribute to an increased propensity to aggregate (2). Due to phosphorylation at serine 129 being one of the most abundant PTMs, several studies reported on the PTM as a potential biomarker (3). Our Alpha Synuclein Ser129 Pre-Formed Fibrils are generated in-vitro from purified phosphorylated monomer and phosphorylation is confirmed with our anti-ASYN pS129 monoclonal antibody (Catalog# SMC-600).
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: 140 aa
- 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: For best results, sonicate immediately prior to use. Refer to the Neurodegenerative Protein Handling Instructions on our website, or the product datasheet for further information. For corresponding monomers, see Catalog# SPR-520. The unphosphorylated construct is Catalog# SPR-322.
Certificate of Analysis: Protein 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 pSer129 Pre-Formed Fibrils (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-521B)
Human Recombinant Alpha Synuclein pSer129 Pre-Formed Fibrils (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-521C)
Human Recombinant Alpha Synuclein pSer129 Pre-Formed Fibrils (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-521E)
Human Recombinant Alpha Synuclein pSer129 Pre-Formed Fibrils (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-521XE)
What is the purity of Alpha Synuclein pSer129 Pre-Formed Fibrils (Human)?
How should Alpha Synuclein pSer129 Pre-Formed Fibrils (Human) be stored?
What expression system was used to produce this protein?
What are the shipping conditions?
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. Fujiwara et al. 2002. α-Synuclein is phosphorylated in synucleinopathy lesions. Nature Cell Biology. DOI: 10.1038/ncb748
3. Magalhaes and Lashuel. 2002. Opportunities and challenges of alpha-synuclein as a potential biomarker for Parkinson’s disease and other synucleinopathies. Npj Parkinsons Disease. DOI: 10.1038/s41531-022-00357-0