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Human Polyclonal ATP6V1H Primary Antibody for ICC, IF - ABIN4282338
Perera, Stoykova, Nicolay, Ross, Fitamant, Boukhali, Lengrand, Deshpande, Selig, Ferrone, Settleman, Stephanopoulos, Dyson, Zoncu, Ramaswamy, Haas, Bardeesy: Transcriptional control of autophagy-lysosome function drives pancreatic cancer metabolism. in Nature 2015
These data provide evidence that partial loss of ATP6V1H function results in osteoporosis/osteopenia.
These studies have uncovered a new, ATP6V1H-mediated pathway that regulates bone formation, and defines a new mechanism of disease that leads to bone loss. We propose that MMP9/MMP13 could be therapeutic targets for patients with this rare genetic disease.
A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.
ATP6V1H may represent a critical molecular mechanism involved in the development of type 2 diabetes and its compilations through its important regulatory effect on vacuolar-ATPase activity.
Data show that the BCG phagosome is relatively depleted in LAMP-2, NPC1, flotillin-1, vATPase, and syntaxin 3.
Our study shows that multiple mechanisms of pump dysfunction result from B1 subunit mutations with a common outcome being defective assembly
Data indicate an important role for the vacuolar-type hydrogen-ATPase and the Golgi apparatus in postendocytic PTH/PTHrP receptor recovery.
Partial loss of ATP6V1H inhibits osteogenic differentiation and promotes adipogenic differentiation of bone marrow stromal cells.
Differences between two isoforms using bioinformatic methods, as well as some in vitro and in vivo methods in mice and zebrafish; found that two isoforms of H subunit showed the tissue specific locations and the ratio of two subunits might have an important role to control osteoclast function and craniofacial development.
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular organelles. V-ATPase-dependent organelle acidification is necessary for multiple processes including protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. The encoded protein is the regulatory H subunit of the V1 domain of V-ATPase, which is required for catalysis of ATP but not the assembly of V-ATPase. Decreased expression of this gene may play a role in the development of type 2 diabetes. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
V-ATPase 50/57 kDa subunits
, V-ATPase subunit H
, V-type proton ATPase subunit H
, nef-binding protein 1
, protein VMA13 homolog
, vacuolar ATP synthase subunit H
, vacuolar ATPase subunit H
, vacuolar proton pump subunit H
, vacuolar proton pump subunit SFD
, ATPase, H+ transporting, lysosomal, V1 subunit H
, 54 kDa vacuolar H(+)-ATPase subunit
, Vacuolar proton pump subunit H
, ATPase, H+ transporting, lysosomal 50/57kDa, V1 subunit H
, V-ATPase H subunit
, vacuolar proton pump H subunit
, un-named hi923
, unm hi923