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ENTPD3 is similar to E-type nucleotidases (NTPases). De plus, nous expédions Ectonucleoside Triphosphate diphosphohydrolase 3 Anticorps (68) et Ectonucleoside Triphosphate diphosphohydrolase 3 Kits (3) et beaucoup plus de produits pour cette protéine.
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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 (Montrer ENTPD2 Protéines) and -3 are ecto (Montrer TRIM33 Protéines)-enzymes expressed in the enteric nervous system. Both enzymes confer protection against gut (Montrer GUSB Protéines) 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 (Montrer ENTPD1 Protéines) 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 (Montrer INS Protéines) secretion by controlling activation of purinergic receptors.
Cystic fibrosis (Montrer S100A8 Protéines) epithelia exhibit >50% lower NTPDase1 (Montrer ENTPD1 Protéines) 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 (Montrer INS Protéines) 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 (Montrer TRIM33 Protéines)-NTPDase3 in trigeminal nociceptive neurons and demonstrated the presence of functional ecto-ATPase (Montrer CEACAM1 Protéines) activity in trigeminal nerves and established that ecto (Montrer TRIM33 Protéines)-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 (Montrer P2RY1 Protéines) signaling.
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 (Montrer ENTPD2 Protéines) and ecto-5'-nucleotidase (Montrer ACPP Protéines), 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