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The results from this analysis indicated that Rab11a (show RAB11A Proteins), Rab11c(Rab25 (show RAB25 Proteins)) and Rab14 were expressed in a wide range of cell lines, including the human placental trophoblastic BeWo cell line.
acst as oncogene (show RAB1A Proteins) and Induces proliferation of gastric cancer cells via AKT (show AKT1 Proteins) signaling pathway
Rab14-specific siRNA-induced downregulation of Rab14 increases the sensitivity to cisplatin, while forced expression of Rab14 lacking 3'-UTR abrogated the pro-apoptotic function of miR (show MLXIP Proteins)-148a in renal cancer cells. miR (show MLXIP Proteins)-148a acts as a tumor suppressor and holds great potential for renal cancer therapy by directly targeting Rab14.
PKCiota binds to Rab14 and that PKCiota requires Rab14 for its correct distribution in cells. As with Rab14, PKCiota protects claudin-2 (show CLDN2 Proteins) from lysosomal degradation and, in consequence, modulates epithelial barrier.
We find that Rab14 indeed binds to RCP, albeit with reduced affinity relative to conventional Rab11-FIP and Rab25-FIP complexes. However, in vivo, Rab11 recruits RCP onto biological membranes.
RAB14 is a direct target of both MIR144 and MIR451. As MIR144 and MIR451 expression increased during human erythropoiesis, RAB14 protein expression decreased. RAB14 as a novel physiological inhibitor of human erythropoiesis.
the miR (show MLXIP Proteins)-451/RAB14 interaction plays an important role in the enhancement of radiosensitivity in NPC (show NPC1 Proteins) cells.
Data indicate that myosin Va (show MYO5A Proteins) interacted with multiple new Rab (show HRB Proteins) subfamilies including Rab6 (show RAB6A Proteins), Rab14 and Rab39B (show RAB39B Proteins).
Rab5a (show RAB5A Proteins), Rab8a (show RAB8A Proteins) and Rab14 are major regulators of MT1-MMP (show MMP14 Proteins) trafficking and invasive migration of primary human macrophages.
Data indicate taht the parasitophorous vacuole (PV), marked with Rab14, Rab30, or Rab43, colocalize with host-derived sphingolipids in the vacuolar space.
clear effect of subcutaneous zoledronic acid administration in vivo on the prenylation of Rab1A (show RAB1A Proteins), Rab5B (show RAB5B Proteins), Rab7A (show RAB7A Proteins) and Rab14 in mouse peritoneal macrophages, confirming that systemic treatment with bisphosphonate drug can inhibit prenylation in myeloid cells in vivo outside the skeleton.
findings provide compelling evidence that Rab22a plays a central role in the MHC-I endocytic trafficking, which is crucial for efficient cross-presentation by dendritic cells
Rab14 limits the sorting of Glut4 (show SLC2A4 Proteins) from endosomes into insulin (show INS Proteins)-sensitive regulated secretory compartments in adipocytes.(
Rab14 activity promotes phagosome maturation during C. albicans infection but is dysregulated on the phagosome in the presence of the invasive hyphal form, which favors fungal survival and escape.
RAB14 functions upstream of RAB10 (show RAB10 Proteins) in the sorting of GLUT4 (show SLC2A4 Proteins) to the specialized transport vesicles that ferry GLUT4 (show SLC2A4 Proteins) to the plasma membrane.
the primary role of Rab14 in GLUT4 (show SLC2A4 Proteins) trafficking is to control the transit of internalised GLUT4 (show SLC2A4 Proteins) from early endosomes into the Golgi complex, rather than direct GLUT4 (show SLC2A4 Proteins) translocation to the plasma membrane.
Data show that Rinl is closely associated with the cytoskeleton and thus contributes to the spatial control of Rab5a and Rab22 signaling at actin-positive compartments.
The kinesin-3 motor KIF16B (show KIF16B Proteins)/Rab14 complex acts in biosynthetic Golgi-to-endosome traffic of the fibroblast growth factor receptor (FGFR) during early embryonic development.
Rab14 enables mycobacterial phagosomes to maintain early endosomal characteristics and avoid late endosomal/lysosomal degradative components.
The complete coding sequences of three porcine genes--RAB14, S35A3 and ITM2A (show ITM2A Proteins) were amplified and nucleotide sequence and tissue expression were analysed.
RAB14 belongs to the large RAB family of low molecular mass GTPases that are involved in intracellular membrane trafficking. These proteins act as molecular switches that flip between an inactive GDP-bound state and an active GTP-bound state in which they recruit downstream effector proteins onto membranes (Junutula et al., 2004
F protein-binding protein 1
, bA165P4.3 (member RAS oncogene family)
, ras-related protein Rab-14
, small GTP binding protein RAB14
, GTPase Rab14
, RAB14, member RAS oncogene family
, rab14, member ras oncogene family
, RAB22, member RAS oncogene family
, ras-related protein Rab-22A