S1071
α-Synuclein A53T human
recombinant, expressed in E. coli, N-terminal histidine tagged, ≥90% (SDS-PAGE), lyophilized powder
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recombinant
expressed in E. coli
Quality Level
Assay
≥90% (SDS-PAGE)
form
lyophilized powder
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Gene Information
human ... SNCA(6622)
General description
α-Synuclein is mapped to human chromosome 4q22.1. It is an intrinsically disordered protein with N-terminal imperfect repeats (KTKEGV), a central NAC crucial for aggregation and an acidic rich flexible C-terminal region.α-Synuclein is present in the Lewy bodies (LBs) and Lewy neurites (LNs).
Application
α-Synuclein A53T human has been used to treat mesencephalic neuronal and stimulate microglial cells prior to reactive oxygen species (ROS) measurement, immunohistochemistry and imaging studies.
Biochem/physiol Actions
α-Synuclein (α-Syn) interacts with toll-like receptor 2 (TLR2) and mediates interleukin-1β (IL-1β) synthesis.
A point mutation in the α-synuclein gene, A53T (Ala53-Thr), is linked to familial Parkinson′s disease. Mice expressing A53T human α-synuclein, but not wild-type or the A30P variants, develop adult-onset neurodegenerative disease with a progressive motoric dysfunction leading to death.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Nathan Meyer et al.
ACS central science, 8(4), 441-448 (2022-05-05)
The detection to α-synuclein (αS) assemblies as a biomarker of synucleinopathies is an important challenge for further development of an early diagnosis tool. Here, we present proof of concept real-time fast amyloid seeding and translocation (RT-FAST) based on a nanopipette
Yan Zhou et al.
Molecular neurodegeneration, 11, 28-28 (2016-04-17)
α-Synuclein (α-Syn), a pathological hallmark of Parkinson's disease (PD), has been recognized to induce the production of interleukin-1β in a process that depends, at least in vitro, on nod-like receptor protein 3 (NLRP3) inflammasome in monocytes. However, the role of
Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala-53? Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice
Lee MK, et al.
Proceedings of the National Academy of Sciences, 99(13), 8968-8973 (2002)
A short motif in the N-terminal region of α-synuclein is critical for both aggregation and function.
Ciaran P A Doherty et al.
Nature structural & molecular biology, 27(3), 249-259 (2020-03-12)
Aggregation of human α-synuclein (αSyn) is linked to Parkinson's disease (PD) pathology. The central region of the αSyn sequence contains the non-amyloid β-component (NAC) crucial for aggregation. However, how NAC flanking regions modulate αSyn aggregation remains unclear. Using bioinformatics, mutation
Imad Abrao-Nemeir et al.
Chemistry, an Asian journal, 17(20), e202200726-e202200726 (2022-08-30)
Solid-state nanopores are an emerging technology used as a high-throughput, label-free analytical method for the characterization of protein aggregation in an aqueous solution. In this work, we used Levodopamine to coat a silicon nitride nanopore surface that was fabricated through
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