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AB5334P Anti-Synuclein α Antibody

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AB5334P
50 µg  
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      Overview

      Replacement Information

      Key Specifications Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      H, RWB, IH(P)ShAffinity PurifiedPolyclonal Antibody
      Description
      Catalogue NumberAB5334P
      Replaces04-1053
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-Synuclein α Antibody
      References
      Product Information
      FormatAffinity Purified
      HS Code3002 15 90
      PresentationAffinity purified immunoglobulin in PBS containing 0.02% sodium azide. Lyophilized. Reconstitute with 50 μL of sterile distilled water. Centrifuge to remove any residue. Glycerol (1:1) can be added for additional stability.
      Quality LevelMQ100
      Applications
      ApplicationDetect Synuclein using this Anti-Synuclein Antibody, α validated for use in WB, IH(P).
      Key Applications
      • Western Blotting
      • Immunohistochemistry (Paraffin)
      Application NotesImmunohistochemistry: 0.5-1 μg/mL on frozen or paraffin sections.

      Western blot: 0.5-1 μg/mL

      Optimal working dilutions must be determined by the end user.
      Biological Information
      ImmunogenSynthetic peptide corresponding amino acids 116-131 of human alpha synuclein.
      HostSheep
      SpecificityRecognizes alpha synuclein.
      Species Reactivity
      • Human
      • Rat
      Antibody TypePolyclonal Antibody
      Entrez Gene Number
      Entrez Gene SummaryAlpha-synuclein is a member of the synuclein family, which also includes beta- and gamma-synuclein. Synucleins are abundantly expressed in the brain and alpha- and beta-synuclein inhibit phospholipase D2 selectively. SNCA may serve to integrate presynaptic signaling and membrane trafficking. Defects in SNCA have been implicated in the pathogenesis of Parkinson disease. SNCA peptides are a major component of amyloid plaques in the brains of patients with Alzheimer's disease. Two alternatively spliced transcripts of SNCA have been identified. Additional splicing may be present but the full-length nature of these variants has not been determined.
      Gene Symbol
      • SNCA
      • PD1
      • alpha-synuclein
      • NACP
      • PARK4
      • MGC110988
      • PARK1
      • Alpha-synuclein
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P37840 # May be involved in the regulation of dopamine release and transport. Soluble protein, normally localized primarily at the presynaptic region of axons, which can form filamentous aggregates that are the major non amyloid component of intracellular inclusions in several neurodegenerative diseases (synucleinopathies). Induces fibrillization of microtubule- associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase 3 activation.
      SIZE: 140 amino acids; 14460 Da
      SUBUNIT: Soluble monomer which can form filamentous aggregates. Interacts with UCHL1 (By similarity). Interacts with phospholipase D and histones.
      SUBCELLULAR LOCATION: Cytoplasm. Membrane. Nucleus. Note=Membrane- bound in dopaminergic neurons. Also found in the nucleus.
      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.
      DOMAIN: SwissProt: P37840 The NAC domain is involved in the fibril formation. The middle region forms the core of the filaments. The C-terminus may regulate aggregation and determine the diameter of the filaments.
      PTM: 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).
      DISEASE: SwissProt: P37840 # Defects in SNCA are a cause of autosomal dominant Parkinson disease 1 (PARK1) [MIM:168601, 168600]. Parkinson disease (PD) is a complex, multifactorial disorder that typically manifests after the age of 50 years, although early-onset cases (before 50 years) are known. PD generally arises as a sporadic condition but is occasionally inherited as a simple mendelian trait. Although sporadic and familial PD are very similar, inherited forms of the disease usually begin at earlier ages and are associated with atypical clinical features. PD is characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology 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. & Defects in SNCA are the cause of Parkinson disease 4 (PARK4) [MIM:605543, 168600]. & Defects in SNCA are the cause of Lewy body dementia (DLB) [MIM:127750]. DLB is a neurodegenerative disorder clinically characterized by dementia and parkinsonism, often with fluctuating cognitive function, visual hallucinations, falls, syncopal episodes, and sensitivity to neuroleptic medication. Presence of Lewy bodies are the only essential pathologic features. & Deposition of fibrillar amyloid proteins intraneuronally as neurofibrillary tangles is characteristic of Alzheimer disease (AD). SNCA is a minor protein found within these deposits, but a major non amyloid component. & Brain iron accumulation type 1 (NBIA1, also called Hallervorden-Spatz syndrome), a rare neuroaxonal dystrophy, is histologically characterized by axonal spheroids, iron deposition, Lewy body (LB)-like intraneuronal inclusions, glial inclusions and neurofibrillary tangles. SNCA is found in LB-like inclusions, glial inclusions and spheroids.
      SIMILARITY: Belongs to the synuclein family.
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsMaintain lyophilized material at -70°C (dry) for up to 12 months. After reconstitution maintain at -20°C in undiluted aliquots for up to 6 months. Avoid repeated freeze/thaw cycles.
      Packaging Information
      Material Size50 µg
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalog Number GTIN
      AB5334P 04053252362903

      Documentation

      Anti-Synuclein α Antibody SDS

      Title

      Safety Data Sheet (SDS) 

      Anti-Synuclein α Antibody Certificates of Analysis

      TitleLot Number
      SHEEP ANTI-ALPHA SYNUCLEIN - 2224384 2224384
      SHEEP ANTI-ALPHA SYNUCLEIN - 3398585 3398585
      SHEEP ANTI-ALPHA SYNUCLEIN - 3785977 3785977
      SHEEP ANTI-ALPHA SYNUCLEIN - 4046566 4046566
      SHEEP ANTI-ALPHA SYNUCLEIN - 4150821 4150821
      SHEEP ANTI-ALPHA SYNUCLEIN -2519273 2519273
      SHEEP ANTI-ALPHA SYNUCLEIN -2689072 2689072
      SHEEP ANTI-ALPHA SYNUCLEIN -2716591 2716591
      SHEEP ANTI-ALPHA SYNUCLEIN -2721482 2721482
      SHEEP ANTI-ALPHA SYNUCLEIN -2761664 2761664

      References

      Reference overviewApplicationPub Med ID
      shRNA targeting α-synuclein prevents neurodegeneration in a Parkinson's disease model.
      Zharikov, AD; Cannon, JR; Tapias, V; Bai, Q; Horowitz, MP; Shah, V; El Ayadi, A; Hastings, TG; Greenamyre, JT; Burton, EA
      The Journal of clinical investigation  125  2721-35  2015

      Show Abstract
      26075822 26075822
      Non-motor parkinsonian pathology in aging A53T α-synuclein mice is associated with progressive synucleinopathy and altered enzymatic function.
      Farrell, KF; Krishnamachari, S; Villanueva, E; Lou, H; Alerte, TN; Peet, E; Drolet, RE; Perez, RG
      Journal of neurochemistry  128  536-46  2014

      Show Abstract
      Immunohistochemistry24117685 24117685
      Neuronal glycogen synthesis contributes to physiological aging.
      Sinadinos, C; Valles-Ortega, J; Boulan, L; Solsona, E; Tevy, MF; Marquez, M; Duran, J; Lopez-Iglesias, C; Calbó, J; Blasco, E; Pumarola, M; Milán, M; Guinovart, JJ
      Aging cell  13  935-45  2014

      Show Abstract
      25059425 25059425
      Higher vulnerability and stress sensitivity of neuronal precursor cells carrying an alpha-synuclein gene triplication.
      Flierl, A; Oliveira, LM; Falomir-Lockhart, LJ; Mak, SK; Hesley, J; Soldner, F; Arndt-Jovin, DJ; Jaenisch, R; Langston, JW; Jovin, TM; Schüle, B
      PloS one  9  e112413  2014

      Show Abstract
      25390032 25390032
      Postmortem 3-D brain hemisphere cortical tau and amyloid-β pathology mapping and quantification as a validation method of neuropathology imaging.
      Smid, LM; Kepe, V; Vinters, HV; Bresjanac, M; Toyokuni, T; Satyamurthy, N; Wong, KP; Huang, SC; Silverman, DH; Miller, K; Small, GW; Barrio, JR
      Journal of Alzheimer's disease : JAD  36  261-74  2013

      Show Abstract
      23568102 23568102
      Expression of human E46K-mutated α-synuclein in BAC-transgenic rats replicates early-stage Parkinson's disease features and enhances vulnerability to mitochondrial impairment.
      Cannon, JR; Geghman, KD; Tapias, V; Sew, T; Dail, MK; Li, C; Greenamyre, JT
      Experimental neurology  240  44-56  2013

      Show Abstract
      Immunofluorescence23153578 23153578
      Nigrostriatal overabundance of α-synuclein leads to decreased vesicle density and deficits in dopamine release that correlate with reduced motor activity.
      Meret Nora Gaugler,Ozgur Genc,Wojciech Bobela,Safa Mohanna,Mustafa Taleb Ardah,Omar Mukhtar El-Agnaf,Marco Cantoni,Jean-Charles Bensadoun,Ralf Schneggenburger,Graham W Knott,Patrick Aebischer,Bernard Laurent Schneider
      Acta neuropathologica  123  2012

      Show Abstract
      22361813 22361813
      A highly reproducible rotenone model of Parkinson's disease.
      Cannon, JR; Tapias, V; Na, HM; Honick, AS; Drolet, RE; Greenamyre, JT
      Neurobiology of disease  34  279-90  2009

      Show Abstract
      19385059 19385059
      Phosphorylation does not prompt, nor prevent, the formation of alpha-synuclein toxic species in a rat model of Parkinson's disease.
      Azeredo da Silveira, S; Schneider, BL; Cifuentes-Diaz, C; Sage, D; Abbas-Terki, T; Iwatsubo, T; Unser, M; Aebischer, P
      Human molecular genetics  18  872-87  2009

      Show Abstract
      19074459 19074459
      Peripheral sensory neurons survive in the absence of alpha- and gamma-synucleins.
      Katerina Papachroni, Natalia Ninkina, Julia Wanless, Anastasios Th Kalofoutis, Nikolai V Gnuchev, Vladimir L Buchman
      Journal of molecular neuroscience : MN  25  157-64  2005

      Show Abstract
      15784963 15784963

      Data Sheet

      Title
      SHEEP ANTI-ALPHA SYNUCLEIN AFFINITY PURIFIED POLYCLONAL ANTIBODY

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