Recombinant Human Alpha-synuclein protein aggregate (Type 2)
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(3 Publications)
Recombinant Human Alpha-synuclein protein aggregate (Type 2) is a Human Full Length protein, in the 1 to 140 aa range, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, FuncS.
View Alternative Names
NACP, PARK1, SNCA, Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor
- FuncS
Supplier Data
Functional Studies - Recombinant Human Alpha-synuclein protein aggregate (Type 2) (AB218817)
TEM of ab218817.
- IHC-P
Supplier Data
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Recombinant Human Alpha-synuclein protein aggregate (Type 2) (AB218817)
Immunohistochemical analysis of 4% formaldehyde fixed primary rat hippocampal neurons from Sprague-Dawley rat labeling lewy body inclusions formed when treated with active Alpha Synuclein Protein Aggregate at 4 μg/ml (D-F), but not when treated with ab218817 at 4 μg/ml (A-C).
Primary antibody : Mouse anti-pSer129 antibody at 1/1000 24 hours at 4°C. Secondary antibody : FITC Goat Anti-Mouse (green) at 1/700 for 1 hours at RT. Counterstain : Hoechst (blue) nuclear stain at 1/4000 for 1 hour at RT. Magnification : 20x.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Alpha-synuclein protein aggregate (Type 2) (AB218817)
SDS-PAGE analysis of ab218817.
Reactivity data
Product details
ab218817 is a protein aggregate which can be used as a control in various assays.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The alpha-synuclein protein plays critical roles in neuronal activity. It contributes to neurotransmitter release regulation by acting in the formation and plasticity of the presynaptic neuronal network. Alpha-synuclein doesn't usually form parts of large protein complexes but it may associate transiently with membranes and vesicular structures. The protein's monomer form has also been observed in alpha lines and related neuronal processes operating alongside various cellular functions.
Pathways
Synaptic vesicle trafficking and dopamine neurotransmitter release are significant areas involving the alpha-synuclein protein. In these pathways alpha-synuclein interacts with other proteins like synaptophysin and protein monomer monomerizations are intrinsic to these processes. Altered function or aggregation of alpha-synuclein disrupts these pathways influencing broader neurological functions.
Specifications
Form
Liquid
Additional notes
ab218817 is purified by ion-exchange and 0.2µm filtered.
General info
Function
The protein expressed by the SNCA gene is involved in various synaptic activities, including the regulation of synaptic vesicle trafficking and neurotransmitter release. As a monomer, it enhances synaptic vesicle exocytosis through vesicle priming, fusion, and dilation of exocytotic fusion pores. Mechanistically, it increases local Ca(2+) release, which is crucial for ATP-induced exocytosis. In its multimeric membrane-bound form, SNCA acts as a molecular chaperone, assisting in the folding of synaptic fusion components known as SNAREs at the presynaptic plasma membrane, in conjunction with cysteine string protein-alpha/DNAJC5, a function that is vital for maintaining normal SNARE-complex assembly during aging. Additionally, SNCA plays a role in dopamine neurotransmission regulation by associating with the dopamine transporter (DAT1) and modulating its activity. This supplementary information is collated from multiple sources and compiled automatically.
Sequence similarities
Belongs to the synuclein family.
Post-translational modifications
Phosphorylated, predominantly on serine residues. Phosphorylation by CK1 appears to occur on residues distinct from the residue phosphorylated by other kinases. Phosphorylation of Ser-129 is selective and extensive in synucleinopathy lesions. In vitro, phosphorylation at Ser-129 promoted insoluble fibril formation. Phosphorylated on Tyr-125 by a PTK2B-dependent pathway upon osmotic stress.. Hallmark lesions of neurodegenerative synucleinopathies contain alpha-synuclein that is modified by nitration of tyrosine residues and possibly by dityrosine cross-linking to generated stable oligomers.. Ubiquitinated. The predominant conjugate is the diubiquitinated form.. Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.
Target data
Publications (3)
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ACS chemical neuroscience 15:2623-2632 PubMed38959406
2024
Applications
Unspecified application
Species
Unspecified reactive species
ACS chemical biology 19:1011-1021 PubMed38517270
2024
Applications
Unspecified application
Species
Unspecified reactive species
Biomolecules 12: PubMed35204664
2022
Applications
Unspecified application
Species
Unspecified reactive species
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