| Field | Specification |
|---|---|
| Accession Number | |
| Alternative Names | A53T mutant alpha synuclein, A53T mutated SNCA, A53T Alpha synuclein monomer, Ala53thr mutant alpha synuclein, Alpha synuclein protein, 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 monomers, SYN protein, Parkinson disease familial 1 Protein |
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| Gene ID | |
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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; native localization: Cytoplasm | Membrane | Nucleus).
Human Recombinant Alpha Synuclein A53T Mutant Monomers (Type 1)
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). The A53T mutation is a missense point mutation where alanine is replaced by threonine at the 53rd amino acid. This mutation has been linked to early-onset Parkinson's Disease and increased rates of alpha synuclein fibrillization.
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: For corresponding PFFs, see catalog# SPR-325
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 A53T Mutant Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-325B)
Human Recombinant Alpha Synuclein A53T Mutant Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-325C)
Human Recombinant Alpha Synuclein A53T Mutant Monomers (StressMarq Biosciences | Victoria, BC CANADA | Catalog# SPR-325E)
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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. 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. Polymeropoulos, M. H. (1998). Science. 276(5321), 2045–2047
8. Conway, K.E., et al. (1998). Nat Med. 4(11):1318-20
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