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Serine/threonine kinase which is able to phosphorylate TAU on serine, threonine and tyrosine residues. Additionally we are shipping tau Tubulin Kinase 1 Proteins (6) and many more products for this protein.
Showing 10 out of 53 products:
Human Polyclonal Ttbk1 Primary Antibody for WB - ABIN1881954
Sato, Xu, Okuyama, Martinez, Walsh, Jacobsen, Swan, Schlautman, Ciborowski, Ikezu: Spatial learning impairment, enhanced CDK5/p35 activity, and downregulation of NMDA receptor expression in transgenic mice expressing tau-tubulin kinase 1. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2009
Show all 2 Pubmed References
Our findings suggest a possible etiology for the two most common frontotemporal lobar degeneration subtypes through a TTBK1/2 activation driven mechanism of neurodegeneration
TTBK1/2 kinases may represent attractive targets for therapeutic intervention for TDP-43 proteinopathies such as Amyotrophic lateral sclerosis and Frontotemporal lobar degeneration-TDP.
X-ray diffraction data were collected and the structure of TTBK1 was determined by molecular replacement both as an apo structure and in complex with a kinase inhibitor
The study suggested that a role for TTBK1 in pre-tangle formation prior to the formation of fibrillar tau and strengthen the idea that tau is phosphorylated at Ser422 at an early/intermediate stage in NFT formation.
TTBK1 may play an important role in the pathogenesis of sporadic late-onset Alzheimer's disease in a Han Chinese population.
This study demonistrated that TTBK1 is a promising new candidate tau phosphorylation-related gene for Alzheimer's disease risk.
TTBK1 in AD brain may be one of the underlying mechanisms inducing CDK5 and calpain activation, NR2B downregulation, and subsequent memory dysfunction.
TTBK1 accelerates motor neuron neurodegeneration by recruiting proinflammatory monocytes and enhancing sensitivity to neurotoxicity in inflammatory conditions.
TTBK1 up-regulation enhances tau phosphorylation and oligomerization, whose toxicity results in enhanced neurodegeneration and locomotor dysfunction in a tauopathy animal model.
Serine/threonine kinase which is able to phosphorylate TAU on serine, threonine and tyrosine residues. Induces aggregation of TAU.
tau-tubulin kinase 1
, brain-derived tau kinase