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BioLegend is proud to offer high quality and specificity reagents for detection of key target proteins involved in the pathogenesis of Parkinson's disease. These reagents include primary antibodies that are highly suitable for use in tissue or cell culture applications, and can be utilized in multiple applications.


Purified anti-α-Synuclein, aggregated

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α-synuclein is expressed principally in the nervous system, but it is also produced in the other tissues, including the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in the presynaptic nerve terminals, interacts with plasma membrane phospholipids, and is also present in the nuclei and mitochondria. At least three isoforms of synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms are α-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-Synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy.

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Purified anti-α-Synuclein Phospho (Ser129)

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α-synuclein is expressed principally in the nervous system, but it is also produced in other tissues, including  the skin. In the brain, the protein is primarily neuronal, but it is also present in glia. Neuronal α-synuclein is concentrated in presynapt   ic nerve terminals, interacts with plasma membrane phospholipids, and is also present in nuclei and mitochondria. At least three isoforms of α-synuclein are produced through alternative splicing. The most common isoform is a 140 amino acid-long transcript. Other isoforms includes, a-synuclein-126, lacking residues 41-54; and α-synuclein-112, which lacks residues 103-130. α-synuclein’s physiological role is poorly understood, but the protein has been implicated in regulating dopamine release and transport, synaptic vesicle clustering, and functioning as a SNARE-complex chaperone. α-synuclein fibrils are a major component of the intracellular Lewy bodies that are associated with Parkinson's disease, Lewy body dementia, and multiple system atrophy. α-synuclein is phosphorylated at low levels under normal physiological conditions whereas the majority of the protein is phosphorylated in Lewy bodies at S129.

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LEGEND MAX™ Human α-Synuclein ELISA Kit

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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.

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Purified anti-PINK1

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PINK1 (PTEN-induced putative kinase 1) is a 63 kD mitochondrial transmembrane protein that is often cleaved by PARL into a 53 kD fragment. The protein is involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). PINK1 phosphorylation of mitochondrial proteins can protect against mitochondrial dysfunction due to cellular stresses. PINK1 mutations can cause autosomal recessive early-onset Parkinson disease.

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Purified anti-DJ-1 (PARK7)

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DJ-1 (PARK7) belongs to the peptidase C56 family of proteins and is expressed in almost all human cells and tissues. DJ-1 is a multi-functional protein associated with mitochondrial function, mitophagy, and male fertility. It acts as an oxidative stress sensor, redox-sensitive chaperone and protease. Therefore, the protein has an important role in cell protection against oxidative stress and cell death. DJ-1 is also associated with prostate cancer, and specific mutations of the protein are linked to autosomal recessive, early onset Parkinson’s disease.

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