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Rabbit Polyclonal Phospho-Synuclein-alpha (Y133) antibody (STJ90680)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, IHC, ELISA
Recommended dilution: WB 1:500-1:2000; IHC 1:100-1:300; ELISA 1:40000;
Recommended protocols: check protocols
Click or hover above images to see image description for Synuclein-alpha (phospho Tyr133) Polyclonal Antibody.
Check alternative names for the antibodyExpand
SNCA antibody, NACP antibody, PARK1 antibody,|Alpha synuclein antibody|Beta synuclein antibody|NACP antibody|Non A beta component of AD amyloid antibody|PARK1 antibody|PARK4 antibody|PD1 antibody|SNCA antibody|SNCB antibody|Synuclein alpha antibody|Synuclein beta antibody|Anti-alpha Synuclein antibody [MJFR1] (ab138501)
SCBT cat No: sc-10717|sc-376010|sc-67321|sc-54758|sc-136385|sc-271066|sc-13991|sc-48349|sc-69699|sc-514908|sc-7012|sc-32281|sc-100291|sc-1477|sc-31358|sc-28982|sc-1476|sc-26416|sc-27136|sc-365559|sc-390884|sc-27099|sc-10721|sc-1475|
Synuclein-alpha (phospho Tyr133) Polyclonal Antibody
|Catalogue No.|| |
Human, Mouse, Rat
Phospho-Synuclein-alpha (Y133) Polyclonal Antibody detects endogenous levels of Synuclein-alpha protein only when phosphorylated at Y133.
Synthesized phospho-peptide derived from Synuclein-alpha (phospho Tyr133) at AA range 60-140
WB, IHC, ELISA
|Recommended dilution|| |
WB 1:500-1:2000; IHC 1:100-1:300; ELISA 1:40000;
|Molecular weight|| |
Synuclein-alpha (phospho Tyr133) Antibody was tube-contained. Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Synuclein-alpha (phospho Tyr133) Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Alpha-synuclein antibody, Non-A beta component of AD amyloid antibody, Non-A4 component of amyloid precursor antibody, NACP antibody
|Protein names|| |
Alpha-synuclein , Non-A beta component of AD amyloid , Non-A4 component of amyloid precursor , NACP
|Protein function|| |
May 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.
|Protein tissue specificity|| |
Expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals.
|Involvement in disease|| |
Note: Genetic 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 (PARK1) [MIM:168601]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features. . Note: The disease is caused by mutations affecting the gene represented in this entry.; Parkinson disease 4 (PARK4) [MIM:605543]: A complex neurodegenerative disorder with manifestations ranging from typical Parkinson disease to dementia with Lewy bodies. Clinical features include parkinsonian symptoms (resting tremor, rigidity, postural instability and bradykinesia), dementia, diffuse Lewy body pathology, autonomic dysfunction, hallucinations and paranoia. Note: The disease is caused by mutations affecting the gene represented in this entry.; Dementia Lewy body (DLB) [MIM:127750]: A neurodegenerative disorder characterized by mental impairment leading to dementia, parkinsonism, fluctuating cognitive function, visual hallucinations, falls, syncopal episodes, and sensitivity to neuroleptic medication. Brainstem or cortical intraneuronal accumulations of aggregated proteins (Lewy bodies) are the only essential pathologic features. Patients may also have hippocampal and neocortical senile plaques, sometimes in sufficient number to fulfill the diagnostic criteria for Alzheimer disease. . Note: The disease is caused by mutations affecting the gene represented in this entry.
|Protein sequence and domain|| |
The ‘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. / Belongs to the synuclein family.
|Protein 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 (By similarity). / Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.
|Protein cellular localization|| |
Cytoplasm > cytosol / Membrane / Nucleus / Cell junction > synapse / Secreted
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St John’s Laboratory Ltd.
|Product type|| |
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