Applications: |
Immunodepletion/Immunocompetition |
Note: |
STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Short Description: |
Alpha Synuclein Blocking Peptide is synthetically produced from the 62-112 sequence and is suitable for use in western blot applications. |
Formulation: |
Liquid form at 2.5mg/ml concentration in PBS. Up to 5% DMSO can be added. Orders with >1mg can be supplied in lyophilized powder form, or in buffer of choice. |
Storage Instruction: |
Store at-20°C for long term storage. Avoid freeze-thaw cycles. |
Gene Symbol: |
SNCA |
Gene ID: |
6622 |
Uniprot ID: |
SYUA_HUMAN |
Immunogen Region: |
62-112 |
Immunogen: |
Synthetic peptide taken within amino acid region 62-112 unique sequence on alpha-synuclein isoform NACP 112 protein. |
Tissue Specificity | Highly expressed in presynaptic terminals in the central nervous system. Expressed principally in brain. |
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. |
Function | Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores. Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis. Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5. This chaperone activity is important to sustain normal SNARE-complex assembly during aging. Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity. |
Peptide Name | Alpha-SynucleinNon-A Beta Component Of Ad AmyloidNon-A4 Component Of Amyloid PrecursorNacp |
Database Links | Reactome: R-HSA-977225 |
Cellular Localisation | CytoplasmMembraneNucleusSynapseSecretedCell ProjectionAxonMembrane-Bound In Dopaminergic NeuronsExpressed And Colocalized With Septin4 In Dopaminergic Axon TerminalsEspecially At The Varicosities |
Alternative Peptide Names | Alpha-Synuclein proteinNon-A Beta Component Of Ad Amyloid proteinNon-A4 Component Of Amyloid Precursor proteinNacp proteinSNCA proteinNACP proteinPARK1 protein |
Information sourced from Uniprot.org
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