This material includes a proprietary 20 amino acids tag before the first Met. The calculated molecular weight is not available. However, in SDS-PAGE gels, this product runs at approximately 15 - 20 kDa as shown below.
S1071
α-Synuclein A53T human
recombinant, expressed in E. coli, N-terminal histidine tagged, ≥90% (SDS-PAGE), lyophilized powder
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500 μG
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500 μG
$506.80
About This Item
$506.80
List Price$724.00Save 30%Web-Only Promotion
Available to ship onMay 01, 2025Details
Request a Bulk Order
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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.[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.[2]α-Synuclein is present in the Lewy bodies (LBs) and Lewy neurites (LNs).[3]
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.[4]
Biochem/physiol Actions
α-Synuclein (α-Syn) interacts with toll-like receptor 2 (TLR2) and mediates interleukin-1β (IL-1β) synthesis.[4]
A point mutation in the α-synuclein gene, A53T (Ala53-Thr), is linked to familial Parkinson′s disease.
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
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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)
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
Mehmet Ozansoy et al.
Molecular neurobiology, 47(2), 460-465 (2012-11-28)
Parkinson's disease (PD) is the second most common neurodegenerative disorder, defined by the presence of resting tremor, muscular rigidity, bradykinesia, and postural instability. PD is characterized by the progressive loss of dopaminergic neurons within the substantia nigra pars compacta of
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
Laura Rueda-Gensini et al.
Frontiers in pharmacology, 13, 905347-905347 (2022-07-16)
Plant-derived products have gained considerable attention as inflammation modulators given the wide variety of anti-inflammatory phytochemicals reported to be present in plants and their limited side effects in vivo during prolonged exposure periods. Non-centrifugal cane sugar (NCS) has been identified
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