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may play a role in exocytosis of neurotransmitters [RGD, Feb 2006].. Additionally we are shipping and many more products for this protein.
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To identify pathological defects in animals expressing the P56S mutant VAPB protein at physiological levels in the appropriate tissues, we have generated Vapb knock-in mice
The disruption of the IRE1 (show ERN1 Proteins)-XBP1 (show XBP1 Proteins) pathway is a cause for the reduced myotube formation in P56S-VAPB-mutation expressing cells.
Vapb knock-out mice exhibit abnormal muscular triacylglycerol levels and FoxO (show FOXO3 Proteins) target gene transcriptional responses to fasting and refeeding
Mice knocked-out for Vapb showed mild motor deficits after 18 months of age.
VapB positively regulates RANKL (show TNFSF11 Proteins)-mediated osteoclastogenesis via PLCgamma2 (show PLCG2 Proteins)-Ca(2 (show CA2 Proteins)+)-NFAT (show NFATC1 Proteins) signaling
Co-expression of mutant protein-associated protein B (show LEPREL2 Proteins) (VAPB) enhances the transactive response DNA-binding protein (show HSF4 Proteins)-43 (TDP-43 (show TARDBP Proteins))-induced motor neuronal cell death while that of wild type-VAPB attenuates it.
Adeno (show ADORA2A Proteins)-associated viral-mediated over-expression of both wild-type and mutated form of human VAPB selectively induces death of primary motor neurons, albeit with different kinetics.
However, VAPBP56S but not VAPBwt transgenic mice develop cytoplasmic TDP-43 (show TARDBP Proteins) accumulations within spinal cord motor neurons that were first detected at 18 months of age.
The total loss of VAPB function in unfolded protein response, induced by one P56S mutant allele, may contribute to the development of P56SVAPB- induced amyotrophic lateral sclerosis.
may play a role in exocytosis of neurotransmitters
, VAMP-associated protein B
, vesicle-associated membrane protein, associated protein B and C
, vesicle-associated membrane protein-associated protein B
, VAMP-associated protein 33b