• Western blot analysis of lysates from mouse brain, using Synuclein (Phospho-Ser129) Antibody. The lane on the right is blocked with the phospho peptide.
  • Immunohistochemistry analysis of paraffin-embedded human brain, using Synuclein (Phospho-Ser129) Antibody. The picture on the right is blocked with the phospho peptide.

Anti-Phospho-SNCA-Ser129 antibody (91-140 aa) (STJ90418)

SKU:
STJ90418

Current Stock:
Host: Rabbit
Applications: WB/IHC/IF/ELISA
Reactivity: Human/Mouse/Rat
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit polyclonal antibody anti-Phospho-Alpha-synuclein-Ser129 (91-140 aa) is suitable for use in Western Blot, Immunohistochemistry, Immunofluorescence and ELISA research applications.
Clonality: Polyclonal
Conjugation: Unconjugated
Isotype: IgG
Formulation: Liquid in PBS containing 50% Glycerol, 0.5% BSA and 0.02% Sodium Azide.
Purification: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Concentration: 1 mg/mL
Dilution Range: WB 1:500-1:2000
IHC 1:100-1:300
ELISA 1:5000
IF 1:50-200
Storage Instruction: Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
Gene Symbol: SNCA
Gene ID: 6622
Uniprot ID: SYUA_HUMAN
Immunogen Region: 91-140 aa
Specificity: Phospho-Synuclein-Alpha (S129) Polyclonal Antibody detects endogenous levels of Synuclein-Alpha protein only when phosphorylated at S129.
Immunogen: The antiserum was produced against synthesized peptide derived from the human Synuclein around the phosphorylation site of Ser129 at the amino acid range 91-140
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.
Protein Name Alpha-Synuclein
Non-A Beta Component Of Ad Amyloid
Non-A4 Component Of Amyloid Precursor
Nacp
Database Links Reactome: R-HSA-977225
Cellular Localisation Cytoplasm
Membrane
Nucleus
Synapse
Secreted
Cell Projection
Axon
Membrane-Bound In Dopaminergic Neurons
Expressed And Colocalized With Septin4 In Dopaminergic Axon Terminals
Especially At The Varicosities
Alternative Antibody Names Anti-Alpha-Synuclein antibody
Anti-Non-A Beta Component Of Ad Amyloid antibody
Anti-Non-A4 Component Of Amyloid Precursor antibody
Anti-Nacp antibody
Anti-SNCA antibody
Anti-NACP antibody
Anti-PARK1 antibody

Information sourced from Uniprot.org

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