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Mammalian Monoclonal PEX5L Primary Antibody for ISt, IHC - ABIN1305011
Zhou, Luo, Lu, Li, Wang, Lu, Xu, He, Guo: Imbalance of HCN1 and HCN2 expression in hippocampal CA1 area impairs spatial learning and memory in rats with chronic morphine exposure. in Progress in neuro-psychopharmacology & biological psychiatry 2014
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Mammalian Monoclonal PEX5L Primary Antibody for ISt, IHC - ABIN1305014
Piskorowski, Santoro, Siegelbaum: TRIP8b splice forms act in concert to regulate the localization and expression of HCN1 channels in CA1 pyramidal neurons. in Neuron 2011
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Mammalian Monoclonal PEX5L Primary Antibody for ISt, IHC - ABIN1305018
Li, Lu, Zhou, Zong, Li, Xu, Guo, Lu: Activation of GABAB receptors ameliorates cognitive impairment via restoring the balance of HCN1/HCN2 surface expression in the hippocampal CA1 area in rats with chronic cerebral hypoperfusion. in Molecular neurobiology 2014
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Mammalian Monoclonal PEX5L Primary Antibody for ISt, IHC - ABIN1305013
Cao-Ehlker, Zong, Hammelmann, Gruner, Fenske, Michalakis, Wahl-Schott, Biel: Up-regulation of hyperpolarization-activated cyclic nucleotide-gated channel 3 (HCN3) by specific interaction with K+ channel tetramerization domain-containing protein 3 (KCTD3). in The Journal of biological chemistry 2013
allosteric coupling of the TRIP8b TPR domains both promotes binding to HCN channels and limits binding to type 1 peroxisomal targeting signal substrates.
TRIP8b competes with a portion of the cAMP-binding site or distorts the binding site by making interactions with the binding pocket, thus acting predominantly as a competitive antagonist that inhibits the cyclic-nucleotide dependence of HCN channels.
the sequential formation of a highly stable trimeric complex involving cargo protein, PEX7 and PEX5L stabilizes cargo binding and is a prerequisite for PTS2-mediated peroxisomal import.
Data show that Rab8b-interacting protein TRIP8b does not compete with cyclic AMP for the same binding region of hyperpolarization activated cyclic nucleotide gated potassium channel 2 (HCN2).
Nedd4-2 plays an important role in the regulation of HCN1 trafficking and may compete with TRIP8b(1a-4) in this process
TRIP8b interacts with the carboxyl-terminal region of HCN channels and regulates their cell-surface expression level and cyclic nucleotide dependence.
Seizure-dependent plasticity wound is not conditional upon TRIP8b in cerebral cortex.
increasing cAMP levels in cells antagonized the up-regulation of HCN1 channels mediated by a TRIP8b construct binding the CNBD exclusively.
This study found that global loss of TRIP8b, a necessary subunit for proper HCN channel localization in pyramidal cells, led to active coping behavior in numerous assays specific to coping style.
This study demonstrated that Hyperpolarization-activated cyclic nucleotide-gated cation (HCN) channels have important functions in controlling neuronal excitability and generating rhythmic oscillatory activity. The role of tetratricopeptide repeat-containing Rab8b-interacting protein (TRIP8b) in regulation of hyperpolarization-activated inward current, I h, in the thalamocortical system and its functional relevance
Study characterized the effects of deletion of the HCN channel auxiliary subunit TRIP8b in the mouse thalamus and cortex, focusing on electrophysiological changes and their role in promoting absence epilepsy
We conclude that TRIP8b in the retina is needed to achieve maximal expression of HCN1.
TRIP8b deletion is not restricted to the integrative properties of neurons but also includes both synaptic and intrinsic plasticity
TRIP8b isoforms are important regulators of HCN1 trafficking in entorhinal neurons.
Study links elevated MMP-2/PEX2 to ischemia and poor wound healing.
Mice lacking TRIP8b demonstrate motor learning deficits and enhanced resistance to multiple tasks of behavioral despair with high predictive validity for antidepressant efficacy.
This study demonstrated that TRIP8b splice isoforms are necessary for the proper trafficking of HCN1 channels to the surface membrane of CA1 pyramidal neurons and for the proper targeting of the channels to the distal dendritic compartment.
These data suggest a possible role for TRIP8b in regulating HCN channel density in the plasma membrane. [TRIP8b]
Both untreated and bile acid-fed PEX2(-/-) mice accumulated high levels of predominantly unconjugated bile acids in plasma because of altered expression of hepatocyte bile acid transporters.
The results suggested that all TRIP8b isoforms inhibit channel opening by shifting activation to more negative potentials. Its functions as an auxiliary subunit that provides a mechanism for the dynamic regulation of HCN1 channel expression and function.
plays a role in cAMP-induced ACTH secretion
peroxisomal biogenesis factor 5-like
, PEX5-related protein
, PEX5-related protein-like
, PEX2-related protein
, PEX5-like protein
, Pex5p-related protein
, peroxin-5-related protein
, peroxisome biogenesis factor 5-like
, tetratricopeptide repeat-containing Rab8b-interacting protein
, peroxin 2
, peroxisomal targeting signal 1 receptor-like
, TPR-containing Rab8b-interacting protein