Key features and details
- Sheep polyclonal to Alpha-synuclein
- Suitable for: WB
- Reacts with: Mouse, Human
- Isotype: IgG
- 倫理基準に準拠 - アニマル・フリーの生産
Alpha-synuclein 一次抗体 製品一覧
製品の詳細Sheep polyclonal to Alpha-synuclein
特異性Human and rat alpha synuclein. Cross reactivity: This antibody is known to react with human, mouse, rat and other rodents. Cross reactivity with other species has not yet been tested.
アプリケーション適用あり: WBmore details
適用なし: Flow Cyt or ICC/IF
種交差性交差種: Mouse, Human
Synthetic peptide corresponding to Human Alpha-synuclein aa 116-131. Synthetic peptide of human synuclein (116-131) coupled to diphtheria toxoid with cysteine residue attached to N-ter of peptide. Conjugate cross-linked by maleimidocaproyl-N-hydroxy succinimide (MSC).
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保存方法Shipped at 4°C. Store at +4°C short term (1-2 weeks). Add glycerol to a final volume of 50% for extra stability and aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Concentration information loading...
精製度Immunogen affinity purified
機能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.
組織特異性Expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals.
関連疾患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
Parkinson disease 4
Dementia Lewy body
配列類似性Belongs to the synuclein family.
ドメイン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.
翻訳後修飾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.
Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.
細胞内局在Cytoplasm, 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
ab6162 は 24 報の論文で使用されています。
- Zhang D et al. Microglial activation contributes to cognitive impairments in rotenone-induced mouse Parkinson's disease model. J Neuroinflammation 18:4 (2021). PubMed: 33402167
- Han C et al. Exosomes from patients with Parkinson's disease are pathological in mice. J Mol Med (Berl) 97:1329-1344 (2019). PubMed: 31302715
- Hou L et al. Lesion of the Locus Coeruleus Damages Learning and Memory Performance in Paraquat and Maneb-induced Mouse Parkinson's Disease Model. Neuroscience 419:129-140 (2019). PubMed: 31634513
- Fragniere AMC et al. Hyperosmotic stress induces cell-dependent aggregation of a-synuclein. Sci Rep 9:2288 (2019). PubMed: 30783136
- Alarcón-Arís D et al. Selective a-Synuclein Knockdown in Monoamine Neurons by Intranasal Oligonucleotide Delivery: Potential Therapy for Parkinson's Disease. Mol Ther 26:550-567 (2018). PubMed: 29273501