EndoClear™ & EndoClear™Plus alpha Synuclein protein
EndoClear & EndoClear Plus
AnaSpec, EGT Group is pleased to offer two EndoClear™ human α-synuclein recombinant proteins. When even lower endotoxin levels are a must, introducing EndoClear™Plus.

 

*previously known as "EndoFree" human recombinant
alpha-synuclein protein

Benefits
  • The lowest endotoxin levels in research grade alpha synuclein

  • Greater than 95% pure

Features
  • Highly Stable

  • Minimizes potential negative
    effects on cell-culture and in-vivo experiments.

  • Thioflavin T binding-Fibrillation proven research grade product (every lot checked for fibrillation capability)

Applications
  • Fibrillation

  • Oligomerization

  • Cell cytotoxicity

About endotoxins

Did you know that Endotoxin can affect cell cultures? Most commercial recombinant proteins produced in bacteria contain inherent/residual endotoxin concentrations1 that create a variety of problems for reseachers using cell culture2-4, not llimited to the following:
Cell Type
 
Endotoxin effects

Human T-cells
Cardiac myocytes
Macrophages
B Lymphomas
Recombinant CHO

 

Induction of proliferation, lymphokine production
Induced contractile dysfunction
Induced IL-6 production
Increased production of immunoglobulin light chains
Altered protein production


Potential sources of endotoxin contamination in cell cultures include, media and its components, water, sera, glassware and plasticware5,6. 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 plastic5,6.

About alpha synuclein

Lewy body in a neuronal cell. Lewy bodies
are abnormal aggregates of α-synuclein
protein observed to develop inside nerve
cells in Parkinson's disease, Lewy body dementia and other disorders8.

α-synuclein is a central molecule responsible for neurodegenerative effects observed in α-synucleopathies and presents as a major component of Lewy bodies in the affected neurons in Parkinson's disease7-10.

It has been hypothesized 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 neurons8.

α-synuclein is a 14.5 kDa (140 amino acids long) protein predominantly expressed in brain, specifically in cerebellum, thalamus, neocortex, hippocampus, and striatum regions7-10.

α-synuclein structure consists of 3 domains,

  • N-terminal (amphipathic) with repeats including KTKEGV consensus sequence important for α-helix formation8.
  • Central hydrophobic region with the non-amyloid component region important for protein aggregation
  • C-terminal region which is highly acidic and proline rich7-10.

 

Related Products
Product Catalog #
EndoClearPlus™ Recombinant Human α - synuclein
EndoClear™* Recombinant Human α - synuclein
Recombinant Human α - synuclein (1 - 140), HiLyte Fluor™488 labeled
Recombinant Human β - synuclein (1 - 134)
Recombinant Human α - synuclein (1 - 140), biotin labeled
SensoLyte® Anti-α-synuclein (Human) ELISA Kit
Recombinant DJ-1 (PARK7) Protein, Human AS-72219-10, -100, -500
Recombinant DJ-1 (PARK7) Protein, Human, GST tagged (GST-DJ-1) AS-72220-10, -100
Assay Kits for Alzheimer's and Parkinsons Disease research Neprilysin, ADAM10 & MORE
Antibodies for Alzheimer's and Parkinsons Disease research Anti-Tau, β-Amyloid, & α-Synuclein
Peptides for Alzheimer's and Parkinsons Disease research β-Amyloid
References

1. Schwartz H, et al. PLOS ONE. 9(12): e13840 (2014)

2. Mattern T, et al. J Immunol. 153: 2996-3004 (1994)

3. Epstein J, et al. In Vitro Cell Dev Biol. 26: 1121-1122 (1990)

4. Morris DD, et al. In Vitro Am J Vet. Res. 53: 1298-1301 (1992)

5. Raetz CRH. Annu Rev Biochem 59: 129-170 (1990)

6. Roslansky PF, et al. J Parental Sci. Tech. 45: 83-87 (1991)

7. Rivers R, et al. Protein Sci. 17: 887-898 (2008).

8. Irwin DJ, et al. Nat Rev Neurosci. 14:626-636 (2013)

9. George MJ. Genome Biology 3, 1, 1-6 (2001).

10. Latawiec D, et al. PLOS ONE. (5)2: e9234 (2010).

11. Irwin JD, et al. Nat Rev Neurosci. 14(9) 626-636: e9234 (2013).