Lewy Body in a Neuronal Cell
Lewy bodies are abnormal aggregates of α-synuclein. They are observed inside nerve cells in Parkinson's disease, Lewy body dementia, and other disorders
- EndoClear™ and EndoClear™ Plus human alpha-synuclein recombinant protein contain exceptional low levels of endotoxin equal to 0.1 EU/µg protein and 0.001 EU/µg protein respectively.
- The lowest endotoxin levels in research-grade alpha-synuclein
- Purity greater than 95%
- Highly stable
- Minimizes potentially negative effects on cell-culture and in vivo experiments
- Thioflavin-T binding fibrillation proven research-grade product (every lot checked for fibrillation capability)
- • Fibrillation
- • Oligomerization
- • Cell cytotoxicity
- Did you know that Endotoxin can affect cell cultures? Most commercial recombinant proteins produced in bacteria contain inherent/residual endotoxin concentrations
that create a variety of problems for researchers using cell culture, not limited to the following:
- Human T-cells ⇒ Induction of proliferation, lymphokine production
- Cardiac myocytes ⇒ Induced contractile dysfunction
- Macrophages ⇒ Induced IL-6 production
- B Lymphomas ⇒ Increased production of immunoglobulin light chains
- Recombinant CHO ⇒ Altered protein production
- Potential sources of endotoxin contamination in cell cultures include media and its components, water, sera, glassware, and plasticware.
Endotoxins are amphipathic molecules with a net negative charge in solution. Their properties include:
- • Heat stability
- • Large aggregate-forming ability
- • Strong affinities to hydrophobic materials like plastic
- Alpha-Synuclein is a central molecule responsible for neurodegenerative effects observed in α-synucleopathies. It presents a major component of Lewy bodies in
affected neurons in Parkinson's disease.
- It is believed that α-synuclein exists - under physiological conditions - in random coils. Under pathological conditions, the native protein undergoes misfolding (beyond proteasomal repair)
to form dimers/trimers/oligomers which in turn aggregate into higher-ordered protofibril structures. These serve as building blocks for pathological inclusions of α-synuclein in the neurons.
- Alpha-Synuclein is a 14.5 kDa (140 amino acids long) protein predominantly expressed in brain, specifically in cerebellum, thalamus, neocortex, hippocampus, and striatum regions.
- Alpha-Synuclein structure consists of 3 domains:
- • N-terminal (amphipathic) with repeats including KTKEGV consensus sequence important for α-helix formation
- • Central hydrophobic region with the non-amyloid component region important for protein aggregation
- • C-terminal region which is highly acidic and proline-rich