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

ALX-804-258-LC05	0.5 ml		263.00 USD
ALX-804-258-L001	1 ml		375.00 USD
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Product Details

Clone:	15G7
Host:	Rat
Isotype:	IgG2a
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

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