alpha-Synuclein: Proteins and Enzymes
alpha -Synuclein is a member of a family of small, soluble proteins that also include beta -, and gamma -Synuclein. alpha -Synuclein is one of the most highly expressed proteins in the human brain. It is predominantly expressed in neurons while lower levels are found in glial cells. alpha -Synuclein protein accumulates in the presynaptic region of nerve terminals where it is thought to play a role in synaptic vesicle biology, but its exact function remains largely unknown. The protein structure cycles between a free, partially unfolded form and a helical, membrane-bound form.
In alpha-Synucleinopathies, protein aggregates containing alpha-Synuclein protein form called Lewy Bodies, glial inclusions, or axonal spheroids depending on the disease. Lewy Bodies are associated with the pathogenesis of Parkinson's disease dimentia. Post-secondary modifications and solubility of alpha -Synuclein are thought to affect Lewy body formation. Phosphorylation level increases before Lewy body formation and increased lipid association of alpha-Synuclein promotes formation as well. alpha -Synuclein protein aggregates have also been found associated with amyloid plaques in Alzheimer's disease. In vitro, alpha -Synuclein oligomers cause neuronal inflammation, degeneration, and cell death. Recombinant alpha -Synuclein protein can be used to study aggregation and toxicity in a controlled environment.
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alpha-Synuclein: Proteins and Enzymes
alpha -Synuclein is a member of a family of small, soluble proteins that also include beta -, and gamma -Synuclein. alpha -Synuclein is one of the most highly expressed proteins in the human brain. It is predominantly expressed in neurons while lower levels are found in glial cells. alpha -Synuclein protein accumulates in the presynaptic region of nerve terminals where it is thought to play a role in synaptic vesicle biology, but its exact function remains largely unknown. The protein structure cycles between a free, partially unfolded form and a helical, membrane-bound form.
In alpha-Synucleinopathies, protein aggregates containing alpha-Synuclein protein form called Lewy Bodies, glial inclusions, or axonal spheroids depending on the disease. Lewy Bodies are associated with the pathogenesis of Parkinson's disease dimentia. Post-secondary modifications and solubility of alpha -Synuclein are thought to affect Lewy body formation. Phosphorylation level increases before Lewy body formation and increased lipid association of alpha-Synuclein promotes formation as well. alpha -Synuclein protein aggregates have also been found associated with amyloid plaques in Alzheimer's disease. In vitro, alpha -Synuclein oligomers cause neuronal inflammation, degeneration, and cell death. Recombinant alpha -Synuclein protein can be used to study aggregation and toxicity in a controlled environment.
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Applications: | IHC, WB, ICC/IF, Func, Bioactivity, +3 More |
Source: | E. coli |
Accession #: | P37840.1 |
Applications: | BA |
Applications: | WB, Func, PAGE, MS, NULL |
Source: | E. coli |
Accession #: | P37840.1 |
Applications: | BA |
Applications: | WB, Func, PAGE |
Applications: | WB, Func, Bioactivity, PAGE |
Applications: | WB, ICC/IF, Func, Bioactivity, PAGE, +2 More |
Applications: | IHC, WB, Func, Bioactivity, PAGE, +1 More |
Applications: | WB, Func, Bioactivity, PAGE |
Applications: | WB, Func, PAGE, MS |
Applications: | WB, Func, PAGE, MS |
Applications: | WB, Func, Bioactivity, PAGE |
Applications: | WB, Func, PAGE, MS |
Applications: | WB, Func, PAGE |
Applications: | WB, Func, PAGE |
Applications: | WB, Func, PAGE, MS |
Applications: | WB, Func, PAGE |
Applications: | WB, Func, PAGE |
Applications: | PAGE |
Applications: | PAGE |