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ENTPD3 is similar to E-type nucleotidases (NTPases). Additionally we are shipping Ectonucleoside Triphosphate diphosphohydrolase 3 Proteins (10) and Ectonucleoside Triphosphate diphosphohydrolase 3 Kits (3) and many more products for this protein.
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expressed in zebrafish hypocretin cells as previously reported in mammals, also in the cranial nerves (gV, gVII, gIV and gX) and in primary sensory neurons (i.e., Rohon-Beard neurons) in the spinal cord
NTPDase2 and -3 are ecto-enzymes expressed in the enteric nervous system. Both enzymes confer protection against gut inflammation in experimental colitis and exhibit alterations in Crohn's disease. These observations suggest that purinergic signalling modulated by E-NTPDases governs neuro-immune interactions that are relevant in Crohn's disease.
Despite the increased level of NTPDase1 and NTPDase3 mRNA expression in chondrogenically induced MSCs, their activity toward ATP remains quite low.
NTPDase3 is the major ectonucleotidase in pancreatic beta-cells in multiple species and modulates insulin secretion by controlling activation of purinergic receptors.
Cystic fibrosis epithelia exhibit >50% lower NTPDase1 activity, protein, and mRNA levels than normal epithelia, whereas these parameters are threefold higher for NTPDase3.
NTPDase3 sequence revealed a high degree of structural fold similarity with a bacterial exopolyphosphatase
efficiently inhibit the NTPDase3expressed in insulin secreting human pancreatic islet cells in situ
Generation of a helical model for NTPDase3 suggests the importance of putative hydrogen bond interactions of conserved polar residues which are critical for enzyme expression, activity, and its susceptibility to membrane perturbations.
Results identified the expression of ecto-NTPDase3 in trigeminal nociceptive neurons and demonstrated the presence of functional ecto-ATPase activity in trigeminal nerves and established that ecto-NTPDase3mediates extracellularATP degradation in the nociceptive lamina on the brainstem.
Mesenteric endothelial cells are primed by schistosomiasis to a pro-inflammatory phenotype characterized by an increased expression of NTPDases 2 and 3, favoring ADP accumulation and mononuclear cell adhesion, possibly contributing to mesenteric inflammation and schistosomiasis morbidity via P2Y1 receptor signaling.
In bladder cancer disease progression there was a weak immunostaining to NTPDase in bladder samples.
The results of this study proposeed that NTPDase3 is a key regulator of nociceptive signaling that also makes an unexpected contribution to innocuous tactile sensation.
the specific localization of NTPDase3 in the digestive system suggests functional roles of the enzyme, in association with NTPDase2 and ecto-5'-nucleotidase, in epithelial functions such as secretion and in enteric neurotransmission.
ENTPD3 is similar to E-type nucleotidases (NTPases). NTPases, such as CD39, mediate catabolism of extracellular nucleotides. ENTPD3 contains 4 apyrase-conserved regions which is characteristic of NTPases.
ectonucleoside triphosphate diphosphohydrolase 3
, ecto-nucleosidase triphosphate diphosphohydrolase 3
, ecto-nucleoside triphosphate diphosphohydrolase 3
, ectonucleoside triphosphate diphosphohydrolase 3-like
, CD39 antigen-like 3
, CD39-like 3
, NTPDase 3
, ecto-ATP diphosphohydrolase 3
, ecto-ATPDase 3
, ecto-ATPase 3
, ecto-apyrase 3