- LB509 (See other available formats)
- Regulatory Status
- Other Names
- NACP, PARK1, PARK4, PD1, Synuclein alpha-140, non-A4 component of amyloid, alpha-synuclein, isoform NACP140, non-A beta component of AD amyloid Parkinson disease (autosomal dominant, Lewy body) 4
- Mouse IgG1, κ
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- Product Citations
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α-synuclein, Alpha-synuclein, is expressed principally in the central nervous system (brain) but is also expressed in low concentrations in a variety of tissues except liver. It is predominantly expressed in the neocortex, hippocampus, substantia nigra, thalamus, and cerebellum of the CNS. It is primarily a neuronal protein, but can also be found in the neuroglial cells. It is concentrated in presynaptic nerve terminals of neurons, as well as having reported nuclear and mitochondrial localization. α-synuclein interacts with plasma membrane phospholipids. α-synuclein in solution is considered to be an intrinsically disordered protein and thus lacks a stable secondary or tertiary structure. However, recent data suggests the presence of partial alpha helical as well as beta sheet structures as well as mostly structured tetrameric states in solution, the equilibrium of which may be altered by binding partners. The human α-synuclein protein is made of 140 amino acids, encoded by the SNCA gene. The primary structure is divided in three distinct domains: (1-60) - An amphipathic N-terminal region dominated by four 11-residue repeats including the consensus sequence KTKEGV. This sequence has a structural alpha helix propensity similar to apolipoproteins-binding domains. (61-95)- a central hydrophobic region which includes the non-amyloid-β component (NAC) region, involved in protein aggregation. (96-140)- a highly acidic and proline-rich region. At least three isoforms of synuclein are produced through alternative splicing. The most common form of the protein, is the full 140 amino acid-long transcript. Other isoforms are alpha-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein may be involved in the regulation of dopamine release and transport and also may function to induce fibrillization of microtubule-associated protein tau. α-synuclein functions as a molecular chaperone in the formation of SNARE complexes. In particular, it can bind to phospholipids of the plasma membrane and to synaptobrevin-2 via its C-terminus domain to influence synaptic activity. α-synuclein is essential for normal development of the cognitive functions and that it significantly interacts with tubulin. It also reduces neuronal responsiveness to various apoptotic stimuli, leading to decreased caspase-3 activation. α-Synuclein fibrils are major substituent of the intracellular Lewy bodies seen in Parkinson's disease.Product Details
- Antibody Type
- Host Species
- Phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide
- The antibody was purified by affinity chromatography and conjugated with biotin under optimal conditions.
- 0.5 mg/mL
- Storage & Handling
- The antibody solution should be stored undiluted between 2°C and 8°C. Do not freeze.
IHC-P - Quality tested
- Recommended Usage
Each lot of this antibody is quality control tested by formalin-fixed paraffin-embedded immunohistochemical staining. For immunohistochemistry, a concentration range of 2 - 10 µg/mL is suggested. It is recommended that the reagent be titrated for optimal performance for each application.
- Application Notes
This antibody is effective in immunoblotting (WB) and formalin-fixed paraffin-embedded immunohistochemical staining (IHC-P).
This antibody reacts with human, but does not react with rodent a-synuclein. The antibody recognizes amino acids 115-122 of human a-synuclein.
(PubMed link indicates BioLegend citation)
- Larson ME, et al. 2012. J Neurosci. 32:10253. (WB) PubMed
- Janezic S, et al. 2013. Proc Natl Acad Sci U S A. 110:E4016. (IHC)
- Iwatsubo T. 2003. J Neurol. 250(3):III11-4.
- Sakamoto M, et al. 2002. Exp Neurol. 177(1):88-94.
- Jakes R, et al. 1999. Neurosci Lett. 269(1):13-6.
- Iwatsubo T. 1999. Rinsho Shinkeigaku 39(12):1285-6. (Japanese)
- Product Citations
AB_2832854 (BioLegend Cat. No. 807709)
AB_2832855 (BioLegend Cat. No. 807710)
- Biology Area
- Cell Biology, Neurodegeneration, Neuroscience, Protein Misfolding and Aggregation
- Molecular Family
- Gene ID
- 6622 View all products for this Gene ID
- View information about alpha-Synuclein 115-121 on UniProt.org
- How many biotin molecules are per antibody structure?
- We don't routinely measure the number of biotins with our antibody products but the number of biotin molecules range from 3-6 molecules per antibody.
|Purified anti-α-Synuclein, 115-121||LB509||IHC-P, WB|
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