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anti-Human RAN Antibodies:
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Human Monoclonal RAN Primary Antibody for ICC, IF - ABIN108658
Nilsen, Rosendal, Sørensen, Wesche, Olsnes, Wiedłocha: A nuclear export sequence located on a beta-strand in fibroblast growth factor-1. in The Journal of biological chemistry 2007
Show all 2 Pubmed References
Human Polyclonal RAN Primary Antibody for ELISA, WB - ABIN4349277
Ly, Wang, Pereira, Rojas, Peng, Feng, Cerione, Wilson: Activation of the Ran GTPase is subject to growth factor regulation and can give rise to cellular transformation. in The Journal of biological chemistry 2010
Human Polyclonal RAN Primary Antibody for ELISA, WB - ABIN250252
Ren, Drivas, DEustachio, Rush: Ran/TC4: a small nuclear GTP-binding protein that regulates DNA synthesis. in The Journal of cell biology 1993
Cow (Bovine) Monoclonal RAN Primary Antibody for ICC, IF - ABIN153125
Simula, Cannizzaro, Canzonieri, Pavan, Maiero, Toffoli, De Re: PPAR signaling pathway and cancer-related proteins are involved in celiac disease-associated tissue damage. in Molecular medicine (Cambridge, Mass.) 2010
The results suggest that HepaCAM and its cytoplasmic domain suppress the nuclear translocation of AR via Ran in prostate cancer (PCa). The cytoplasmic domain of HepaCAM may serve as a novel target for therapy in PCa.
Our data has shown that GEMIN3 gene (rs197388) polymorphisms might be associated with a risk of POAG development in the Polish population. This is the first report evaluating the polymorphic variants of miRNA processing genes, RAN and GEMIN3, with a changed risk of glaucoma.
DICER rs3742330 AG+GG genotype was associated with more advanced T stage compared to AA genotype ( P=0.009). More patients with XPO5 rs2257082 CC genotype had poorly differentiated tumors compared with CT+TT genotype carriers..), carriers of RAN rs14035 CC genotype had higher three-year OS rate than carriers of CT+TT genotype (adjusted HR 3.174; 95% CI 1.010, 9.973; P=0.048).
Taken together, the results provide strong in vitro evidence of the involvement of Ran in the progression of breast cancer and suggest that it could have high potential as a therapeutic target and/or marker of disease.
Molecular structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A has been reported.
The mobility of Emerin depends on RanGTP. In cells overexpressing YFP-Emerin, the mobility of YFP-Emerin was higher in Samp1 knock out cells and lower in cells overexpressing Samp1, suggesting that Samp1 significantly attenuates the mobility of Emerin in the nuclear envelope.The affinity between Samp1 and Emerin is decreased in the presence of Ran, suggesting that Ran attenuates the interaction between Samp1 and Emerin.
KPNB1 and Ran protein jointly mediated the nuclear import of NDV M protein, showing that KPNB1 protein interacted with NDV M protein to form binary complex and then entered into the nucleus with the assistance of Ran protein.
Ran GTPase promotes cancer progression via Met recepto-rmediated downstream signaling
Data show that the distribution of components of the ras-related nuclear protein (Ran) pathway that influence microtubule behaviors is determined by their interactions with microtubules, resulting in microtubule nucleators being localized by the microtubules whose formation they stimulate.
The RAS-related nuclear protein ((P) ran), breast cancer metastasis suppressor 1 ((P) brms1) and minichromosome maintenance complex component 5 ((P) mcm5) promoters have the specificity and strength needed for cancer-specific expression-targeted gene therapy.
Authors found that decreasing Ran-GTP levels or tethering active Ran to the equatorial membrane affects anillin's localization and causes cytokinesis phenotypes.
lysine-acetylation regulates nearly all aspects of Ran-function such as RCC1 catalyzed nucleotide exchange, intrinsic nucleotide hydrolysis, its interaction with NTF2 and the formation of import- and export-complexes.
These results showed that BLM enters the nucleus via the importin beta1, RanGDP and NTF2 dependent pathway, demonstrating for the first time the nuclear trafficking mechanism of a DNA helicase.
RAN Translation Regulated by Muscleblind Proteins in Myotonic Dystrophy Type 2
we demonstrated that DICER (rs3742330) and RAN (rs14035) were associated with the survival of HCC patients
RAN translation from antisense CCG repeats generates novel proteins that accumulate in ubiquitinated inclusions in Fragile X-associated tremor/ataxia syndrome patients.
interaction of Samp1 and Ran in the inner nuclear membrane
RAN role in cell cycle, DNA repair and DNA damage-induced cell senescence
Binding of Ran to NTF2 is required for NTF2 to inhibit nuclear expansion and import of large cargo molecules.
RAN is pivotal in linking spatiotemporal control of centrosome regulators to the cell cycle machinery.
Depleting TPX2 decreases microtubule formation frequency specifically at the tip and the base of the neurite, and these correlate precisely with the regions where active GTP-bound Ran proteins are enriched.
Data suggest Ran activation by RanBP1 in macrophages promotes Legionella phagosome formation and phagocytosis; LegG1 functions as bacterial Ran activator, localizes to phagosomes, and promotes microtubule stabilization, phagocytosis, and replication.
Augmented expression of Ran in progranulin-deficient neurons restores nuclear TDP-43 levels and improves their survival.
Reduction in Ran levels causes cytoplasmic decrease and nuclear accumulation of importin alpha leading to cellular senescence in normal cells.
a novel connection between the hyper-activation of the small GTPase Ran and the matricellular protein SMOC-2 that has important consequences for oncogenic transformation.
A critical function of RanBP2 is to capture recycling RanGTP-importin-beta complexes at cytoplasmic fibrils to allow for adequate classical nuclear localization signal-mediated cargo import.
Downregulation of the Ran GTPase effector RanBP1 is required for nuclear reorganisation.
intracellular Ran protein levels controlled the nuclear presence of certain transcription factors
Activation of the Ran GTPase is subject to growth factor regulation and can give rise to cellular transformation.
intracellular Ran protein levels control the nuclear retention for selective transcription factors such as c-Jun and c-Fos of AP-1, which is known to be critical in T cell activation and proliferation and lymphokine secretion.
RAN expression in mouse embryo
expression of Ran/M1 and Ran/M2 increased in pachytene spermatocytes with progressive transcript accumulation until they reached the round spermatid stage, in the seminiferous epithelium of adults
RanGDP is regulated by phosphorylation and regulated by NTF2
Tax directly binds Ran and Ran-binding protein-1, locates to centrosomes/spindle poles, and causes supernumerary centrosomes
meiosis II spindle assembly did not tolerate changes in the level of RanGTP
Induction of apoptosis in murine neuroblastoma by systemic delivery of transferrin-shielded siRNA polyplexes for downregulation of Ran is reported.
Results demonstrate that Ran is associated with the resistance to and tolerance of multiple pesticides.
RanGTP is required for meiotic spindle organization and the initiation of embryonic development.
the Canoe Ras-association (RA) domains directly bind RanGTP
Knockdown of the small G protein Ran, which is essential for nuclear transport, leads to an arrest of EcR in the cytoplasm, but does not prevent efficient nuclear import of the most important heterodimerization partner of EcR, ultraspiracle (Usp).
the possibility that Dntf-2r and ran-like might be involved in genomic conflicts during spermatogenesis
results demonstrate that distinctly from its role in spindle assembly, RanGTP maintains spindle microtubules in anaphase through the local activation of ISWI and that this is essential for proper chromosome segregation
gtpase ran localizes around the microtubule spindle in vivo during mitosis in Drosophila embryos
anillin and Peanut are involved in pseudocleavage furrow ingression in syncytial embryos, a process that is regulated by Ran
RAN (ras-related nuclear protein) is a small GTP binding protein belonging to the RAS superfamily that is essential for the translocation of RNA and proteins through the nuclear pore complex. The RAN protein is also involved in control of DNA synthesis and cell cycle progression. Nuclear localization of RAN requires the presence of regulator of chromosome condensation 1 (RCC1). Mutations in RAN disrupt DNA synthesis. Because of its many functions, it is likely that RAN interacts with several other proteins. RAN regulates formation and organization of the microtubule network independently of its role in the nucleus-cytosol exchange of macromolecules. RAN could be a key signaling molecule regulating microtubule polymerization during mitosis. RCC1 generates a high local concentration of RAN-GTP around chromatin which, in turn, induces the local nucleation of microtubules. RAN is an androgen receptor (AR) coactivator that binds differentially with different lengths of polyglutamine within the androgen receptor. Polyglutamine repeat expansion in the AR is linked to Kennedy's disease (X-linked spinal and bulbar muscular atrophy). RAN coactivation of the AR diminishes with polyglutamine expansion within the AR, and this weak coactivation may lead to partial androgen insensitivity during the development of Kennedy's disease.
GTP-binding nuclear protein Ran
, GTPase Ran
, androgen receptor-associated protein 24
, guanosine triphosphatase Ran
, member RAS oncogene family
, ras-like protein TC4
, ras-related nuclear protein
, RAN, member RAS oncogene family
, RAN, member RAS oncogene family pseudogene 1
, Ran GTPase