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Rabbit Anti-SNCA Antibody (CSB-PA021912DSR1HU)
Supplier: CUSABIO BIOTECH CO.
Non-A beta component of AD amyloid Antibody,Non-A4 component of amyloid precursor Antibody, NACP Antibody,SNCA Antibody,NACP Antibody, PARK1 AntibodyMore alternative names for the antibody
BCSG1 antibody|beta synuclein antibody|Breast cancer specific gene 1 protein antibody|Gamma synuclein antibody|NACP antibody|PARK1 antibody|Persyn antibody|PRSN antibody|SNCA antibody|SNCB antibody|SNCG antibody|SR antibody|Synoretin antibody
Anti-gamma Synuclein antibody (ab55424)
Anti-gamma Synuclein antibody (ab55424)
Recommended applications: ELISA, IHC
Recommended dilution: Recommended dilution:IHC:1:20-1:200
Recommended protocols: check protocols
|Catalogue No.|| |
Recombinant human Alpha-synuclein protein (61-140AA)
|Recommended dilution|| |
|Molecular weight|| |
Antigen Affinity Purified
Shipped at 4 Celcius Degree. Upon delivery aliquot and store at -20 Celcius Degree or -80 Celcius Degree. Avoid repeated freeze.
|Database links|| |
Entrez Gene:6623( Human), Entrez Gene:20618( Mouse), Entrez Gene:64347( Rat), Omim:602998( Human), SwissProt:O76070( Human), SwissProt:Q9Z0F7( Mouse), SwissProt:Q63544( Rat), Unigene:349470( Human), Unigene:282800( Mouse), Unigene:2883( Rat)
|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, autosomal dominant (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, autosomal dominant (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|| |
Belongs to the synuclein family. 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.
|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 . Note=Membrane-bound in dopaminergic neurons. .
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|Product type|| |
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