Recombinant Rabbit monoclonal primary
Recombinant Phospho alpha Synuclein (S129) Monoclonal Antibody (ET7107-30)
Synthetic phospho-peptide corresponding to residues surrounding ser129 of human alpha synuclein.
Hela, HUVEC, SH-SY-5Y, rat brain tissue, human kidney tissue, mouse brain tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
NACP, SNCA, NACP, PARK1
Belongs to the synuclein family.
Highly expressed in presynaptic terminals in the central nervous system. Expressed principally in brain.
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 (By similarity).; Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.
Cytoplasm. Membrane. Nucleus. Cell junction, synapse. Secreted. Note=Membrane-bound in dopaminergic neurons.
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. Plays also a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity.