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α-Synuclein (human) monoclonal antibody (15G7)

ALX-804-258-LC05 0.5 ml 270.00 USD
ALX-804-258-L001 1 ml 386.00 USD
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Product Details

Immunogen:Synthetic peptide corresponding to aa 116-131 of human α-synuclein.
UniProt ID:P37840
Species reactivity:Human
Crossreactivity:Does not cross-react with mouse α-synuclein or recombinant β- or γ-synuclein.
Applications:IHC (FS), IHC (PS), IP, WB
Recommended Dilutions/Conditions:Immunohistochemistry (paraffin sections, 1:5-1:10)
Western Blot (1:5)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
Formulation:Liquid. Hybridoma supernatant containing 0.05% sodium azide.
Handling:Aliquot diluted antibody into smaller volumes prior to freezing. Avoid freeze/thaw cycles.
Shipping:Blue Ice
Short Term Storage:+4°C
Long Term Storage:-20°C
Scientific Background:Synuclein was originally identified in Torpedo californica as a small neuroprotein that localized to the nuclear envelope of neurons and to presynaptic nerve termini. The human homolog was initially termed NACP, a precursor protein to NAC (Non-Ab Component), because of its prevalence in amyloid plaques in Alzheimer’s patients. Later, NACP was recognized as being α-synuclein (α-SYN), a 14kDa protein, belonging to the synuclein family of phosphoproteins that also includes: β-synuclein, γ-synuclein, and synoretin.
α-SYN is recognized as a key component in the development and diagnosis of neurodegenerative synucleinopathic diseases (NSDs), such as Alzheimer’s and Parkinson’s disease. In the past five years, several genetic and post-translational modifications to α-SYN have been elucidated that have been linked to its collaboration in the formation of the classical Lewy bodies (LBs) or Lewy neurites that are associated with neurodegeneration. A study that shed more light on the neurogenesis of autorecessive synucleinopathies (ARSs) was the finding that α-SYN accumulation can occur due to mutations in the E3 ubiquitin ligase.
ARSs only account for a small percentage of NSD. Thus the illustration that α-SYN has a high susceptibility to tyrosine nitration may be the key component in understanding the formation of LBs. Due to the chemical structure of α-SYN, tyrosine nitration readily leads to the formation of oligomers via covalent O,O’-dityrosine bonds (cross-linking). Nitrosylated, wild-type, α-SYN products thus form SDS-insoluble, heat-stable aggregates in vitro that may account for α-SYN inclusions in all forms of NSDs.
Regulatory Status:RUO - Research Use Only

Product Literature References

Alpha synuclein processing by MMP-3 - implications for synucleinopathies: A. Bluhm, et al.; Behav. Brain Res. 434, 114020 (2022), Abstract;
Generation of a homozygous and a heterozygous SNCA gene knockout human-induced pluripotent stem cell line by CRISPR/Cas9 mediated allele-specific tuning of SNCA expression: Y. Schneider, et al.; Stem Cell Res. 65, 102952 (2022), Abstract;
O-GlcNAcase Inhibitor ASN90 is a Multimodal Drug Candidate for Tau and α-Synuclein Proteinopathies: B. Permanne, et al.; ACS Chem. Neurosci. 13, 1296 (2022), Abstract;
Transplantation of Adipose-Derived Stem Cells Alleviates Striatal Degeneration in a Transgenic Mouse Model for Multiple System Atrophy: C. Chang, et al.; Cell Transplant. 29, 963689720960185 (2020), Abstract; Full Text
Anle138b modulates α-synuclein oligomerization and prevents motor decline and neurodegeneration in a mouse model of multiple system atrophy: A. Heras-Garvin, et al.; Mov. Disord. 34, 255 (2019), Abstract;
Translational inhibition of α-synuclein by Posiphen normalizes distal colon motility in transgenic Parkinson mice: Y.M. Kuo, et al.; Am. J. Neurodegener. Dis. 8, 1 (2019), Abstract; Full Text
Treadmill exercise intervention improves gait and postural control in alpha-synuclein mouse models without inducing cerebral autophagy: G. Minakaki, et al.; Behav. Brain Res. 363, 199 (2019), Abstract;
Abrogating Native α-Synuclein Tetramers in Mice Causes a L-DOPA-Responsive Motor Syndrome Closely Resembling Parkinson's Disease: S. Nuber, et al.; Neuron 100, 75 (2018), Abstract;
Limited effects of dysfunctional macroautophagy on the accumulation of extracellularly derived α-synuclein in oligodendroglia: implications for MSA pathogenesis: L. Fellner, et al.; BMC Neurosci. 19, 32 (2018), Abstract; Full Text
Refolding of helical soluble α-synuclein through transient interaction with lipid interfaces: M. Rovere, et al.; FEBS Lett. 592, 1464 (2018), Abstract;
Early and progressive microstructural brain changes in mice overexpressing human α-Synuclein detected by diffusion kurtosis imaging: A. Khairnar, et al.; Brain Behav. Immun. 61, 197 (2017), Abstract;
Long-term oral kinetin does not protect against α-synuclein-induced neurodegeneration in rodent models of Parkinson's disease: A.L. Orr, et al.; Neurochem. Int. 109, 106 (2017), Abstract; Full Text
Subcellular Parkinson’s Disease-Specific Alpha-Synuclein Species Show Altered Behavior in Neurodegeneration: R. Abdullah, et al.; Mol. Neurobiol. 54, 7639 (2017), Abstract;
Changes in the miRNA-mRNA Regulatory Network Precede Motor Symptoms in a Mouse Model of Multiple System Atrophy: Clinical Implications: S. Schafferer, et al.; PLoS One 11, e0150705 (2016), Application(s): Immunohistochemistry, Abstract; Full Text
High-content analysis of α-synuclein aggregation and cell death in a cellular model of Parkinson's disease: F. Macchi, et al.; J. Neurosci. Methods 261, 117 (2016), Application(s): Western blot, Abstract;
α-Synuclein-induced myelination deficit defines a novel interventional target for multiple system atrophy: B. Ettle, et al.; Acta Neuropathol. 132, 59 (2016), Abstract; Full Text
Involvement of Peripheral Nerves in the Transgenic PLP-α-Syn Model of Multiple System Atrophy: Extending the Phenotype: D. Kuzdas-Wood, et al.; PLoS One 10, e0136575 (2015), Application(s): Immunohistochemistry, Abstract; Full Text
Noninvasive bioluminescence imaging of α-synuclein oligomerization in mouse brain using split firefly luciferase reporters: S.A. Aelvoet, et al.; J. Neurosci. 34, 16518 (2014), Application(s): Immunocytochemistry and Western Blot on neuroblastoma cells (SHSY5Y), Abstract;
Behavioral characterization of A53T mice reveals early and late stage deficits related to Parkinson's disease: K.L. Paumier, et al.; PLoS One 8, e70274 (2013), Application(s): IHC using trangenic mouse tissue, Abstract; Full Text
Bladder dysfunction in a transgenic mouse model of multiple system atrophy: M. Boudes, et al.; Mov. Disord. 28, 347 (2013), Abstract;
Intact olfaction in a mouse model of multiple system atrophy: F. Krismer, et al.; PLoS One 8, e64625 (2013), Application(s): IHC using mouse tissue, Abstract; Full Text
Toll-like receptor 4 is required for α-synuclein dependent activation of microglia and astroglia: L. Fellner, et al.; Glia 61, 349 (2013), Application(s): ICC using mouse cell, Abstract; Full Text
Alpha-synuclein aggregation involves a bafilomycin A 1-sensitive autophagy pathway: J. Klucken, et al.; Autophagy 8, 754 (2012), Application(s): ICC using human cells, Abstract; Full Text
Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis: V.M. Nemani, et al.; Nat Med. 65, 66 (2010), Abstract; Full Text
Clinicopathologic study of a SNCA gene duplication patient with Parkinson disease and dementia: T. Obi, et al.; Neurology 70, 238 (2008), Abstract;
Alpha-synuclein overexpression increases cytosolic catecholamine concentration: E.V. Mosharov, et al.; J. Neurosci. 26, 9304 (2006), Abstract; Full Text
Lipid rafts mediate the synaptic localization of alpha-synuclein: D.L. Fortin, et al.; J. Neurosci. 24, 6715 (2004), Abstract;
Elevation of beta-amyloid peptide 2-42 in sporadic and familial Alzheimer's disease and its generation in PS1 knockout cells: J. Wiltfang, et al.; J. Biol. Chem. 276, 42645 (2001), Abstract; Full Text
Subcellular localization of wild-type and Parkinson's disease-associated mutant alpha-synuclein in human and transgenic mouse brain: P.J. Kahle, et al.; J. Neurosci. 20, 6365 (2000), Abstract; Full Text
Synuclein accumulation in a case of neurodegeneration with brain iron accumulation type 1 (NBIA-1, formerly Hallervorden-Spatz syndrome) with widespread cortical and brainstem-type Lewy bodies: M. Neumann, et al.; Acta Neuropathol. 100, 568 (2000), Abstract;

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