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Rab3d is required for Xenopus anterior neurulation by regulating Noggin (show NOG ELISA Kits) secretion.
Loss of Rab3D from secretory vesicles, leading to disproportionate Rab27 (show RAB27A ELISA Kits)-to-Rab3D activity, may contribute to the enhanced release of cathepsin S (show CTSS ELISA Kits) in tears of patients with Sjogren's syndrome.
Data suggest that both microtubule-associated DYNLT (dynein light chain Tctex-type 1) and cytoplasmic DYNLT (dynein 1 intermediate chain 2 DYNC1LI2) are equally able to bind to small GTPases Rab3D (Rab3d GTPase) and RagA (Ras-related GTP binding A).
Acute expression of Rab1 and Rab3d DN constructs partially alleviated this negative feedback mechanism and resulted in impaired ER to Golgi trafficking of procollagen.
Targeted disruption of Tctex-1 by RNA interference significantly impairs bone resorption capacity and mislocalizes Rab3D vesicles in osteoclasts.
MIST1 binds to highly conserved CATATG E-boxes to directly activate transcription of 6 genes, including those encoding the small GTPases RAB26 and RAB3D.
Rab3D plays an important role in regulating the terminal steps of acinar exocytosis and this effect is greatest on the early phase of amylase (show AMY ELISA Kits) release.
Rab3D is not required for exocrine exocytosis but for maintenance of secretory granules size.
Rab3D has a role in binding GTP (show AK3 ELISA Kits) in pancreatic acini
Data suggest that Rab3D modulates a post-trans-Golgi network trafficking step that is required for osteoclastic bone resorption.
Rab3-induced modifications to primed vesicles causes a transient increase in the transduction efficacy of synaptic action potential trains and optimizes the encoding of synaptic information at an intermediate spike frequency range.
targeting the Rab3D may be a potential therapeutic target for treatment of esophageal squamous cell carcinoma.
increased Rab3D expression is associated with invasiveness of CRC (show CALR ELISA Kits) cells
High expression of small GTPase Rab3D promotes cancer progression and metastasis.
The presence of Rab3D(N135I) decreases the restriction of maturing secretory granules (SGs (show FBN1 ELISA Kits)) to the F-actin-rich cell cortex, blocks the removal of the endoprotease furin (show FURIN ELISA Kits) from SGs (show FBN1 ELISA Kits) and impedes the processing of the luminal SG protein secretogranin II (show SCG2 ELISA Kits).
Our findings indicate that Rab3D regulates the exocytosis of many components critical for the maintenance of oral physiology.
mutant Rab3D proteins interfere with the formation of bona fide Weibel-Palade bodies and consequently the acute, histamine-induced release of von-Willebrand factor (show VWF ELISA Kits)
Protein transport. Probably involved in vesicular traffic (By similarity). May be involved in the insulin-induced exocytosis of glut4-containing vesicles in adipocytes.
RAB3D, member RAS oncogene family
, Ras-related protein Rab-3D
, ras-related protein rab-3d
, ras-related protein Rab-3D
, Rab3D upregulated with myeloid differentiation
, glioblastoma overexpressed
, GTP-binding protein Rab-3D