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Study shows that, when uropathogenic E. coli infect bladder epithelial cells, they are targeted by autophagy but avoid degradation because of their capacity to neutralize lysosomal pH. This change is detected by TRPML3, TRPML3 activation then spontaneously initiates lysosome exocytosis, resulting in expulsion of exosome-encased bacteria.
Trpml3 inactivation does not lead to hearing and vestibular impairment in mice
Results describe the expression and subcellular distribution of TRPML3 in the inner ear as well as in other sensory organs.
prominent role for MCOLN3 in regulating Ca(2 (zeige CA2 Antikörper)+) homeostasis at the endosomal pathway
Mutations are associated with deafness and pigmentation defects in varitint-waddler (Va) mice
there is a hierarchy controlling the subcellular distributions of the TRPMLs such that TRPML1 (zeige MCOLN1 Antikörper) and TRPML2 (zeige MCOLN2 Antikörper) dictate the localization of TRPML3 and not vice versa
TRPML3 is critical for stereocilia bundle formation during development and may function during endocytosis or exocytosis.
This study provides the first direct mechanistic link of a mutation in a TRPML3 with mammalian hearing loss.
TRPML3(A419P) and (I362T+A419P) at physiological potentials may have a role in hair cell degeneration and deafness
The varitint-waddler mouse phenotypes and the TRPML3 ion channel mutation: cause and consequence. (Review)
these results suggest that TRPML3 plays a role in autophagosome maturation through the interaction with GATE16 (zeige GABARAPL2 Antikörper), by providing Ca(2 (zeige CA2 Antikörper)+) in the fusion process.
TRPML3 and TRPV5 (zeige TRPV5 Antikörper) heteromers could have a biological function
Negatively charged amino acids in the extracellular loops of TRPML3 may interfere with the observed sodium inhibition.
TRPML 1 (zeige MCOLN1 Antikörper), 2 and 3 assemblies regulated cell viability and starvation-induced autophagy.
analysis of the TRPML3 channel pore and its stable expansion by the Varitint-Waddler-causing mutation
First characterization of wild-type TRPML3 calcium-permeable channel properties and its regulation by extracytosolic (luminal)hydrogen ion (H+).
The deaf-waddler (zeige ATP2B2 Antikörper) isoform of PMCA2 (zeige ATP2B2 Antikörper), operating at 30% efficacy, showed a significantly decreased ability to rescue the Ca(2 (zeige CA2 Antikörper)+) loading of cells expressing TRPML3(A419P).
Results show that mucolipin 3 is a novel calcium channel that plays a crucial role in the regulation of cargo trafficking along the endosomal pathway.
This gene encodes one of members of the mucolipin cation channel proteins. Mutation studies of the highly similar protein in mice have shown that the protein is found in cochlea hair cells, and mutant mice show early-onset hearing loss and balance problems. Multiple transcript variants encoding different isoforms have been found for this gene.