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Your Position: Home > Protein > Alpha-synuclein > ALN-H51H4

Human Alpha-Synuclein Pre-formed Fibrils Protein, His Tag (ThT active)

  • Synonym
    NACP, PARK1, PARK4, PD1
  • Source
    Human Alpha-Synuclein Pre-formed Fibrils, His Tag(ALN-H51H4) is expressed from E.coli cells. It contains AA Met 1 - Ala 140 (Accession # P37840-1 ).
    Predicted N-terminus: Met 1
  • Molecular Characterization
    Alpha-synuclein Structure

    This protein carries a polyhistidine tag at the C-terminus

    The protein has a calculated MW of 16.3 kDa.

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >90% as determined by SDS-PAGE.

  • Formulation

    Supplied as 0.2 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Shipping

    This product is supplied and shipped as sterile liquid solution with dry ice, please inquire the shipping cost.

  • Storage

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. The product should be stored at -70°C or room temperature for short storage. Do not store fibrils on ice or at 4°C;
    2. The unsonicated fibril is validated to be stable after storage at -70°C for 1 year under sterile conditions;
    3. The sonicated fibril should be stored at -70°C for not more than 8 weeks.
SDS-PAGE
Alpha-synuclein SDS-PAGE

Alpha-Synuclein monomer on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 90%.

Bioactivity-ThT Assay
 Alpha-synuclein THT

Thioflavin T is a sensitive fluorescence reporter of fibrils formulation that binds to beta sheet-rich structures. The alpha synuclein pre-formed fibrils (Cat. No. ALN-H51H4) is able to induce the aggregation of alpha synuclein monomers (Cat. No. ALN-H52H8) (QC tested).

Electron Microscope
 Alpha-synuclein ELECTRON MICROSCOPE

Transmission electron microscopy (TEM) of alpha-synuclein preformed fibrils (Cat. No. ALN-H51H4). Fibril structure is visible on negative stain TEM images of ALN-H51H4 (Routinely tested).

  • Background
    Alpha-synuclein is a neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. It acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DJC5. Abnormalities in alpha-synuclein are implicated in the pathogenesis of Parkinsons disease (PD). Alpha-synuclein is present in Lewy-bodies, the neuropathological hallmark of PD, and the protein and its aggregation have been widely linked to neurotoxic pathways that ultimately lead to neurodegeneration.
  • Clinical and Translational Updates
  • Please contact us via TechSupport@acrobiosystems.com if you have any question on this product.

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  • Number of Drugs in Clinical Trials:12 Details
  • Latest Research Phase:Phase 3 Clinical

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