36-011
Anti-nitro-α/β-Synuclein Antibody, clone nSyn12
clone nSyn12, Upstate®, from mouse
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
antibody form
ascites fluid
antibody product type
primary antibodies
clone
nSyn12, monoclonal
species reactivity
human
manufacturer/tradename
Upstate®
technique(s)
immunohistochemistry: suitable
western blot: suitable
NCBI accession no.
shipped in
dry ice
Gene Information
human ... SNCA(6622)
Specificity
α-Synuclein nitrated at Tyr125 and Tyr136
β-Synuclein nitrated at Tyr130
β-Synuclein nitrated at Tyr130
Application
Anti-nitro-α/β-Synuclein Antibody, clone nSyn12 is an antibody against nitro-α/β-Synuclein for use in WB, IH.
Quality
rountinely evaluated on recombinant protein nitrated in vitro
Target description
α-Synuclein, Mr 14.5kDa
β-Synuclein, Mr 17kDa
β-Synuclein, Mr 17kDa
Physical form
Format: Unpurified
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Certificates of Analysis (COA)
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Ashley D Reynolds et al.
Journal of neurochemistry, 104(6), 1504-1525 (2007-11-27)
Microglial neuroinflammatory processes play a primary role in dopaminergic neurodegeneration for Parkinson's disease (PD). This can occur, in part, by modulation of glial function following activation by soluble or insoluble modified alpha-synuclein (alpha-syn), a chief component of Lewy bodies that
Bregje W M de Wildt et al.
Biotechnology and bioengineering, 120(7), 2013-2026 (2023-05-06)
The transition in the field of bone tissue engineering from bone regeneration to in vitro models has come with the challenge of recreating a dense and anisotropic bone-like extracellular matrix (ECM). Although the mechanism by which bone ECM gains its
B I Giasson et al.
The Journal of biological chemistry, 274(12), 7619-7622 (1999-03-13)
alpha-Synuclein is a soluble presynaptic protein which is pathologically redistributed within intracellular lesions characteristic of several neurodegenerative diseases. Here we demonstrate that wild type and two mutant forms of alpha-synuclein linked to familial Parkinson's disease (Ala30 --> Pro and Ala53
J M Souza et al.
The Journal of biological chemistry, 275(24), 18344-18349 (2000-04-05)
Intracellular proteinaceous aggregates are hallmarks of many common neurodegenerative disorders, and recent studies have shown that alpha-synuclein is a major component of several pathological intracellular inclusions, including Lewy bodies in Parkinson's disease (PD) and glial cell inclusions in multiple system
Emilio Fernández-Espejo et al.
Antioxidants (Basel, Switzerland), 10(5) (2021-06-03)
Background. Salivary α-synuclein (aSyn) and its nitrated form, or 3-nitrotyrosine-α-synuclein (3-NT-αSyn), hold promise as biomarkers for idiopathic Parkinson's disease (IPD). Nitrative stress that is characterized by an excess of 3-nitrotyrosine proteins (3-NT-proteins) has been proposed as a pathogenic mechanism in
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