CATALOG PROTEINS

Neuroscience Recombinant Proteins

Tau - Alzheimer's Disease (AD) Research


Tau is a microtubule-associated protein that stabilizes and promotes microtubule assembly.
In the human brain, it is present as six isoforms that are 352, 381, 383, 410, 412, and 441 amino acids in length (1-5).

The longest form (Tau-441) contains 441 amino acids.
When hyperphosphorylated, it can detach and form paired helical filament (PHF) aggregates (2-5).


PHFs were found in neurofibrillary tangles in Alzheimer's disease (AD) patients, making a strong link between Tau hyperphosphorylation and AD.
Tau can undergo glycosylation in the same regions where phosphorylation takes place leading to the hypothesis that Tau glycosylation may help stabilizing microtubule-Tau assemblies and prevent free Tau aggregation (5).
The sequence (Accession # AAC04279.1) corresponds to the full length human Tau-441 (2N4R isoform) and was expressed in E.coli.

Parkinson's Disease (PD) Research


Alpha-Synuclein is a 140 amino acid protein abundant in the brain, where it may be involved in the control of neurotransmitter release and regulate the release of dopamine. It has the potential to aggregate and form insoluble fibrils in pathogenic conditions such as Parkinson’s Disease, where it represents a major component of Lewy bodies.6-9 This aggregation process may lead to synaptic dysfunction.


The Sequence (Accession# NP_000336) corresponds to the full length human alpha-synuclein protein without an affinity tag and was expressed in E. coli.


DJ-1 (Parkinson disease protein 7) also known as PARK7 is a 189-amino acid protein that is ubiquitously expressed in many organs including brain, liver, kidney, pancreas, heart, and others10-14.
Although DJ-1 was originally discovered as a novel oncogene product, it was found to play several other roles in biological processes. This includes the regulation of RNA binding activity, fertility, anti-oxidative stress, and is linked to the early onset of Parkinson’s Disease when mutated10-14.
Sequence (Accession# NP_001116849) corresponds to the full-length human DJ-1 protein ±N-terminal GST tag and was expressed in E. coli.

Multiple Sclerosis (MS) & EAE (Experimental autoimmune encephalomyelitis) Research


MOG, Myelin Oligodendrocyte Glycoprotein (MOG) is a member of the immunoglobulin superfamily and is expressed exclusively in central nervous system (CNS).
Although MOG protein constitutes only 0.01-0.05% of the CNS myelin proteins, it was demonstrated that MOG protein is a crucial autoantigen for multiple sclerosis in humans and experimental autoimmune encephalomyelitis (EAE) in rodents and monkeys.
Human (Accession# CAQ10087), mouse (Accession# NP_034944) and rat (Accession# CAE84068) sequences were derived from the extracellular domain of MOG and were expressed in E. coli. These recombinant proteins contain a 6x His tag.


Beta-synuclein belongs to the family of highly conservative proteins in vertebrates.
Similar to alpha-synuclein, beta-synuclein is found primarily in the brain; however, unlike alpha-synuclein, it is not associated with Lewy bodies in Parkinson disease 6-8.
Recent investigations demonstrated that beta-synuclein can induce mild experimental autoimmune encephalomyelitis (EAE) in Lewis rats.
Sequence (Accession# NP_003076) corresponds to the human beta-synuclein along with a 6x His tag and was expressed in E. coli.

References 

  1. Bulic, B., et al. Neuropharmacol 59, 276 (2010)
  2. Voss, K., et al. Mol Neurodegen 4, 1 (2009)
  3. Rankin, CA.,et al. Mol Neurodegen 2, 1 (2007)
  4. Patterson, KR. et al. J Biol Chem 286, 23063 (2011)
  5. Wang, Y., et al. Biochem Soc Trans 38, 955 (2010)
  6. Rivers, R. et al. Protein Science 17, 887 (2008)
  7. Bruening, W. et al. Cancer. 88, 9, 2154 (2000)
  8. George, M. J. Genome Biology 3, 1 (2001)
  9. Latawiec, D. et al. PloS ONE 5, 2, 1 (2010)
  10. Huai, Q. et al. FEBS Letters 549, 171 (2003)
  11. Inden, M. et al. J Pharma Sci 117, 189 (2011)
  12. Kitamura, Y. et al. Mol Neurodegener 6, 1 (2011)
  13. Chen, J. et al. Hum Mol Genetics 19, 2395 (2010)
  14. Andres-Mateos, E., et al. Proc Nat Acad Sci 104, 14807 (2007)