Alpha-synuclein (phospho S129) peptide
Be the first to review this product! Submit a review
|
(6 Publications)
Alpha-synuclein (phospho S129) peptide is a Synthetic blocking peptide.
View Alternative Names
NACP, PARK1, SNCA, Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor
Reactivity data
Product details
- If the peptide doesn't dissolve try an organic solvent e.g. DMSO, then dilute using water or buffer.
- Consider that any solvent used must be compatible with your assay. If a peptide does not dissolve and you need to recover it, lyophilise to remove the solvent.
- Gentle warming and sonication can effectively aid peptide solubilisation. If the solution is cloudy or has gelled the peptide may be in suspension rather than solubilised.
- Peptides containing cysteine are easily oxidised, so should be prepared in solution just prior to use.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Specifications
Form
Lyophilized
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 (6)
Recent publications for all applications. Explore the full list and refine your search
Brain : a journal of neurology 147:444-457 PubMed38006313
2023
Applications
Unspecified application
Species
Unspecified reactive species
ACS measurement science au 2:485-492 PubMed36785659
2022
Applications
Unspecified application
Species
Unspecified reactive species
Acta neuropathologica communications 10:98 PubMed35794636
2022
Applications
Unspecified application
Species
Unspecified reactive species
Acta neuropathologica 142:807-825 PubMed34453582
2021
Applications
Unspecified application
Species
Unspecified reactive species
BMC complementary medicine and therapies 20:73 PubMed32143619
2020
Applications
Unspecified application
Species
Unspecified reactive species
Acta neuropathologica 135:877-886 PubMed29536165
2018
Applications
IHC-P
Species
Human
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com