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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
predicted mol wt 145-151 kDa
species reactivity
human, mouse
technique(s)
immunofluorescence: suitable
immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... TTBK1(84630)
General description
Tau tubulin kinase (TTBK1) belongs to the casein kinase 1 superfamily and is involved in the phosphorylation of specific serine/threonine residues in paired helical filaments of the tau protein. It is specifically expressed in the brain and induces tau aggregation in human neuronal cells in a dose-dependent manner. TTBK1 levels have been found to be upregulated in the brains of Alzheimer′s disease (AD) patients, and mice expressing human TTBK1 protein showed significant age-dependent memory impairment. These mice displayed increased levels of the CDK5 activators p25 and p35, and reduced levels of the NMDA receptor types 2B and 2D, suggesting that TTBK1 may play a role in memory dysfunction in AD patients. Multiple isoforms of TTBK1 are known to exist. This antibody is predicted to not cross-react with TTBK2.
Tau tubulin kinase 1 (TTBK1) is a serine/threonine and tyrosine kinase. It belongs to the casein kinase 1 superfamily and is neuron-specific. The encoded protein has a kinase domain, a unique polyglutamate domain and several PEST (proline–glutamate–serine–threonine) sequences. The gene encoding TTBK1 is localized on human chromosome 6p21.1.
Immunogen
TTBK1 antibody was raised against a 16 amino acid peptide near the carboxy terminus of human TTBK1.
Application
Anti-TTBK1 antibody produced in rabbit has been used in western blotting.
Biochem/physiol Actions
Tau tubulin kinase 1 (TTBK1) is responsible for phosphorylation of TDP-43 (TAR DNA binding protein), a protein associated with amyotrophic lateral sclerosis and frontotemporal lobar dementia. High expression or abundance of TTBK1 might be associated with neurodegeneration in these diseases. It also phosphorylates tau protein and might be associated with Alzheimer′s disease progression.
Features and Benefits
Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.
Physical form
Supplied at approx. 1 mg/mL in phosphate buffered saline containing 0.02% sodium azide.
Other Notes
The action of this antibody can be blocked using blocking peptide SBP3500002.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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The tau tubulin kinases TTBK1/2 promote accumulation of pathological TDP-43.
Liachko NF
PLoS Genetics (2014)
The structure of human tau-tubulin kinase 1 both in the apo form and in complex with an inhibitor.
Kiefer SE
Acta Crystallographica. Section F, Structural Biology Communications (2014)
Nicole F Liachko et al.
PLoS genetics, 10(12), e1004803-e1004803 (2014-12-05)
Pathological aggregates of phosphorylated TDP-43 characterize amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP), two devastating groups of neurodegenerative disease. Kinase hyperactivity may be a consistent feature of ALS and FTLD-TDP, as phosphorylated TDP-43 is not observed in the
The Tau Tubulin Kinases TTBK1/2 Promote Accumulation of Pathological TDP-43
Nicole F
PLoS Genetics (2014)
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