Key features and details
- Rabbit polyclonal to Alpha-synuclein (phospho Y136)
- Suitable for: ICC/IF, WB
- Reacts with: Mouse, Rat, Human
- Isotype: IgG
Product nameAnti-Alpha-synuclein (phospho Y136) antibody
See all Alpha-synuclein primary antibodies
DescriptionRabbit polyclonal to Alpha-synuclein (phospho Y136)
SpecificityDue to high sequence homology ab194775 might react with Beta synuclein
Tested applicationsSuitable for: ICC/IF, WBmore details
Species reactivityReacts with: Mouse, Rat, Human
Synthetic peptide corresponding to Human Alpha-synuclein (C terminal) (phospho Y136). Phospho specific peptide corresponding to residues surrounding Tyrosine 136 of Human alpha Synuclein.
Database link: P37840
- Mouse brain tissue extract; HeLa cells.
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Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Storage bufferpH: 7.30
Preservative: 0.02% Sodium azide
Constituents: 50% Glycerol, 49% PBS
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab194775 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|ICC/IF||1/100 - 1/200.|
|WB||1/500 - 1/2000. Predicted molecular weight: 14 kDa.|
FunctionMay be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation.
Tissue specificityExpressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals.
Involvement in diseaseGenetic alterations of SNCA resulting in aberrant polymerization into fibrils, are associated with several neurodegenerative diseases (synucleinopathies). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer disease amyloid plaque, and a major component of Lewy body inclusions. They are also found within Lewy body (LB)-like intraneuronal inclusions, glial inclusions and axonal spheroids in neurodegeneration with brain iron accumulation type 1.
Parkinson disease 1
Parkinson disease 4
Dementia Lewy body
Sequence similaritiesBelongs to the synuclein family.
DomainThe 'non A-beta component of Alzheimer disease amyloid plaque' domain (NAC domain) is involved in fibrils formation. The middle hydrophobic region forms the core of the filaments. The C-terminus may regulate aggregation and determine the diameter of the filaments.
modificationsPhosphorylated, 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.
Cellular localizationCytoplasm, cytosol. Membrane. Nucleus. Cell junction, synapse. Secreted. Membrane-bound in dopaminergic neurons.
- Information by UniProt
- Alpha synuclein antibody
- Alpha-synuclein antibody
- Alpha-synuclein, isoform NACP140 antibody
All lanes : Anti-Alpha-synuclein (phospho Y136) antibody (ab194775) at 1/500 dilution
Lane 1 : Mouse brain tissue extract with blocking peptide
Lane 2 : Mouse brain tissue extract
Predicted band size: 14 kDa
Immunofluorescent analysis of methanol-fixed HeLa cells labeling alpha Synuclein (phospho Y136) with ab194775 at 1/100 dilution.
ab194775 has not yet been referenced specifically in any publications.