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AB9850 Anti-phospho-α Synuclein (Ser129) Antibody

This Anti-phospho-α Synuclein (Ser129) Antibody is validated for use in WB for the detection of phospho-α Synuclein (Ser129).

Anti-phospho-α Synuclein (Ser129) Antibody: Ficha de datos de seguridad (MSDS o SDS), certificado de análisis y de calidad (CoA y CoQ), expedientes, folletos y otros documentos disponibles.
Research Category: Neuroscience Research Sub-Category: Neurodegenerative Diseases Gene Symbol: SNCA, MGC110988, PD1, alpha-synuclein, NACP, PARK1, PARK4, Alpha-synuclein UniProt Number: P37840
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AB9850
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      Tabla espec. clave

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      RWBRbAffinity PurifiedPolyclonal Antibody
      Description
      Catalogue NumberAB9850
      Replaces04-1052
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-phospho-α Synuclein (Ser129) Antibody
      References
      Product Information
      FormatAffinity Purified
      PresentationLiquid in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug/mL BSA and 50% glycerol.
      Quality LevelMQ100
      Applications
      ApplicationThis Anti-phospho-α Synuclein (Ser129) Antibody is validated for use in WB for the detection of phospho-α Synuclein (Ser129).
      Key Applications
      • Western Blotting
      Biological Information
      ImmunogenSynthetic peptide of amino acids surrounding the phosphoSerine 129 site of rat alpha synuclein.
      HostRabbit
      SpecificityAlpha Synuclein, phospho Serine 129. The antibody recognizes a protein of ~15 kDa corresponding to alpha synuclein, phospho Serine 129 in lysates from rat cortex. Immunolableing is blocked by preadsorption with the phospho-peptide used as the immunogen but not by the corresponding dephospho-peptide.
      Species Reactivity
      • Rat
      Species Reactivity NoteThe immunogen has 100% homology with human, mouse, non-human primate, bovine and canine.
      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
      • MGC110988
      • PD1
      • alpha-synuclein
      • NACP
      • PARK1
      • PARK4
      • Alpha-synuclein
      Modifications
      • Phosphorylation
      Purification MethodImmunoAffinity Purified
      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 at -20degC in undiluted for up to 6 months after date of receipt. Avoid repeated freeze/thaw cycles. Do not store in a self defrosting freezer.
      Packaging Information
      Material Size100 µL
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Número de referencia GTIN
      AB9850 04053252729201

      Documentation

      Anti-phospho-α Synuclein (Ser129) Antibody Ficha datos de seguridad (MSDS)

      Título

      Ficha técnica de seguridad del material (MSDS) 

      Anti-phospho-α Synuclein (Ser129) Antibody Certificados de análisis

      CargoNúmero de lote
      RABBIT ANTI-ALPHA SYNUCLEIN, phospho Serine 129 - 3206402 3206402
      RABBIT ANTI-ALPHA SYNUCLEIN, phospho Serine 129 - 3385702 3385702
      RABBIT ANTI-ALPHA SYNUCLEIN, phospho Serine 129 - 4081586 4081586
      RABBIT ANTI-ALPHA SYNUCLEIN, phospho Serine 129 - 4158352 4158352
      RABBIT ANTI-ALPHA SYNUCLEIN, phospho Serine 129 -2571250 2571250
      RABBIT ANTI-ALPHA SYNUCLEIN, phospho Serine 129 AFFINITY PURIFIED POLYCLONAL ANTIBODY 2886898
      RABBIT ANTI-ALPHA SYNUCLEIN, phospho Serine 129 AFFINITY PURIFIED POLYCLONAL ANTIBODY - 2004530 2004530
      RABBIT ANTI-ALPHA SYNUCLEIN, phospho Serine 129 AFFINITY PURIFIED POLYCLONAL ANTIBODY - 2010059 2010059
      RABBIT ANTI-ALPHA SYNUCLEIN, phospho Serine 129 AFFINITY PURIFIED POLYCLONAL ANTIBODY - 2051762 2051762
      RABBIT ANTI-ALPHA SYNUCLEIN, phospho Serine 129 AFFINITY PURIFIED POLYCLONAL ANTIBODY - 2191064 2191064
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      Referencias bibliográficas

      Visión general referenciasPub Med ID
      Alpha-synuclein phosphorylation enhances eosinophilic cytoplasmic inclusion formation in SH-SY5Y cells
      Smith, Wanli W, et al
      J Neurosci, 25:5544-52 (2005)  2004

      		15944382 15944382
      Effects of alpha-synuclein immunization in a mouse model of Parkinson's disease
      Masliah, Eliezer, et al
      Neuron, 46:857-68 (2005)  2004

      		15953415 15953415
      Misfolded proteinase K-resistant hyperphosphorylated alpha-synuclein in aged transgenic mice with locomotor deterioration and in human alpha-synucleinopathies
      Neumann, Manuela, et al
      J Clin Invest, 110:1429-39 (2002)  2002

      		12438441 12438441
      Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein
      Okochi, M, et al
      J Biol Chem, 275:390-7 (2000)  1999

      		10617630 10617630

      Ficha técnica

      Cargo
      RABBIT ANTI-ALPHA SYNUCLEIN, phospho Serine 129 AFFINITY PURIFIED POLYCLONAL ANTIBODY

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      Categorías

      Life Science Research > Antibodies and Assays > Primary Antibodies