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Protein transport. Additionally we are shipping RAB3D Antibodies (37) and RAB3D Kits (1) and many more products for this protein.
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Human RAB3D Protein expressed in Escherichia coli (E. coli) - ABIN667481
Baldini, Hohl, Lin, Lodish: Cloning of a Rab3 isotype predominantly expressed in adipocytes. in Proceedings of the National Academy of Sciences of the United States of America 1992
Rab3d is required for Xenopus anterior neurulation by regulating Noggin (show NOG Proteins) secretion.
Loss of Rab3D from secretory vesicles, leading to disproportionate Rab27 (show RAB27A Proteins)-to-Rab3D activity, may contribute to the enhanced release of cathepsin S (show CTSS Proteins) in tears of patients with Sjogren's syndrome.
Data suggest that both microtubule-associated DYNLT (dynein light chain Tctex-type 1 (show DYNLT1 Proteins)) and cytoplasmic DYNLT (dynein 1 intermediate chain 2 DYNC1LI2 (show DYNC1LI2 Proteins)) are equally able to bind to small GTPases Rab3D (Rab3d GTPase (show RACGAP1 Proteins)) and RagA (Ras-related GTP binding A (show RRAGA Proteins)).
Acute expression of Rab1 (show RAB1A Proteins) 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 (show DYNLT1 Proteins) 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 (show RAB26 Proteins) 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 Proteins) release.
Rab3D is not required for exocrine exocytosis but for maintenance of secretory granules size.
Rab3D has a role in binding GTP (show AK3 Proteins) in pancreatic acini
Data suggest that Rab3D modulates a post-trans-Golgi network trafficking step that is required for osteoclastic bone resorption.
Rab3 (show RAB3A Proteins)-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.
High expression of small GTPase (show RACGAP1 Proteins) Rab3D promotes cancer progression and metastasis.
The presence of Rab3D(N135I) decreases the restriction of maturing secretory granules (SGs (show FBN1 Proteins)) to the F-actin-rich cell cortex, blocks the removal of the endoprotease furin (show FURIN Proteins) from SGs (show FBN1 Proteins) and impedes the processing of the luminal SG protein secretogranin II (show SCG2 Proteins).
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 Proteins)
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