Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
Alle Spezies anzeigen
Weitere Synonyme anzeigen
Wählen Sie die Spezies und Applikation aus
anti-Mouse (Murine) Antikörper:
anti-Rat (Rattus) Antikörper:
Sie gelangen zu unserer vorgefilterten Suche.
Cow (Bovine) Polyclonal RANBP2 Primary Antibody für IHC (p), IHC - ABIN266970
Hamard, Boyer-Guittaut, Camuzeaux, Dujardin, Hauss, Oelgeschläger, Vigneron, Kedinger, Chatton: Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity. in Nucleic acids research 2007
Show all 2 Pubmed References
Human Polyclonal RANBP2 Primary Antibody für IP, WB - ABIN408616
Wang, Yan, Liu, Liu, Lin, Liu, Chen, Zhang, Xu, Shi, Li, Zhao, Meng, Xia, Li, Zhu: HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal misfolded Blimp-1s in lymphoma cells. in Nature communications 2017
Human Polyclonal RANBP2 Primary Antibody für ICC, IF - ABIN3201003
Yokoyama, Hayashi, Seki, Panté, Ohba, Nishii, Kuma, Hayashida, Miyata, Aebi: A giant nucleopore protein that binds Ran/TC4. in Nature 1995
We describe three in vitro reconstituted disassembly intermediates, which show binding of a Crm1 export complex via two FG-repeat patches, cargo-release by RanBP2's Ran-binding domains and retention of free Crm1 at RanBP2 after Ran-GTP hydrolysis.
RAN binding protein 2 increase the sumoylation of cyclin-dependent kinase inhibitor 1B in cholangiocarcinoma cell line QBC939.
Importin-beta and CRM1 control a RANBP2 spatiotemporal switch essential for mitotic kinetochore function.
Translocation of p53 is regulated by androgen-dependent sumoylation mediated by the G3BP2-interacting SUMO-E3 ligase, RanBP2. G3BP2 knockdown results in reduced tumor growth and increased nuclear p53 accumulation in mouse xenograft models of prostate cancer with or without long-term androgen deprivation.
These our results reveal spatio-temporal regulation in the recruitment of nucleoporins and translation factors to cytoplasmic viral factories , and particularly the importance of Nup358 in vaccinia virus infection.
NUSAP1 contributes to accurate chromosome segregation by acting as a co-factor for RanBP2-RanGAP1-UBC9 during cell division.
Nup358-AGO interaction is important for miRNA-mediated gene silencing and identifies SIM as a new interacting motif for the AGO family of proteins.
recurrent or familial ANE without the RANBP2 mutation has a more severe outcome and greater predilection for male sex than that with the RANBP2 mutation. This suggests that there are unknown gene mutations linked to ANE.
Based on the literature review of ANE1 with RANBP2 mutation, we propose a threshold for RANBP2 mutation tes
findings indicate that RanGDP and not RanGTP is the physiological target for the RanBP2 SUMO E3 ligase complex
Taken together, topographic and functional interactions between dynactin, importin-beta and RanBP2 are involved in nuclear translocation of IGF-1R.
analysis of the RANBP2-ALK gene fusion identified in ALK-positive diffuse large B-cell lymphoma with a unique nuclear membrane staining of ALK protein
Nup358, a nucleoporin that forms the cytoplasmic filaments of the nuclear pore complex, plays an important role in the nuclear import of hTERT.
Our data show that Nup358 supports nuclear transport functions important for cellular homeostasis and for HIV-1 nuclear import
Case Report/Review: RANBP2-ALK gene rearrangement in inflammatory myofibroblastic tumors.
RANBP2-ALK fusion combined with monosomy 7 may be related to a unique clonal hematologic disorder of childhood and adolescence, characterized by myelomonocytic leukemia and a poor prognosis [case report/ review]
Mitotic arrest and the following cell death were caused by depletion of RanBP2.
Isomerization by NUP358 may be preserved by HIV-1 to target the nuclear pore and synchronize nuclear entry with capsid uncoating.
The translation of a subset of mRNAs encoding secretory proteins is potentiated by RanBP2.
These findings reveal novel roles of Ranbp2 in the modulation of intrinsic and extrinsic cell death mechanisms and pathways
These results demonstrate a function of RanBP2-mediated SUMOylation of SHP in maintaining bile acids (BA) homoeostasis and protecting from the BA hepatotoxicity.
results demonstrate that Ranbp2 controls nucleocytoplasmic, chemokine and metalloproteinase 28 signaling, and proteostasis of substrates that are crucial to motoneuronal homeostasis and whose impairments by loss of Ranbp2 drive ALS-like syndromes
RanBP2 expression was regulated by Zap70.
Data (including data from studies in transgenic/knockout mice) suggest that Ranbp2 in photoreceptor neurons participates in coupling of photoreceptor degeneration (neural dysmorphology) and apoptosis (neural death) caused by toxic exposure to light.
These studies unravel selective roles of Ranbp2 and its RBD2 and RBD3 in retinal pigment epithelium survival and functions.
These results unveil distinct mechanistic and biological links between prolyl isomerase and chaperone activities of Ranbp2 cyclophilin toward proteostasis.
Novel roles in Ran GTPase-independent subdomains of RBD2 and RBD3, and KBD of RanBP2, confer antagonizing and multi-modal mechanisms of kinesin-1 activation and regulation of mitochondrial motility.
Ranbp2 haploinsufficiency is associated with metabolic imbalances leading to parkinson's disease.
Knockdown of RANBP2 specifically affected the late step of nuclear entry, inducing cytoplasmic granules enriched with phosphorylated components. This suggests a novel regulatory mechanism for nuclear speckle formation involving RANBP2 and phosphorylation.
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.
findings indicate that the nuclear pore complex undergoes dynamic remodeling during muscle cell differentiation and that Nup358 is prominently involved in the remodeling process
These results provide a rationale for the neuroprotection from light damage of photosensory neurons by RANBP2 insufficiency.
RanBP2 associates in vitro and in vivo and colocalizes with the mitochondrial metallochaperone, Cox11, and the pacemaker of glycolysis, hexokinase type I (HKI) via its leucine-rich domain.
binding of the kinesin-binding domain of RanBP2 to KIF5B and KIF5C determines mitochondria localization and function
these data identify RanBP2 as a chromosomal instability gene that regulates Topo IIalpha by sumoylation and suppresses tumorigenesis.
The RAN binding protein 2-dependent production of free fatty acids or metabolites promote apoptosis of photoreceptors in concert with the light-stimulated production of reactive oxygen species.
reports identification of the cyclophilin-related protein, RanBP2 (note at the time the protein was not designated RanBP2), and the cis-trans prolyl isomerase activity of its cyclophilin domain
reports interaction of the RBD4 and CY domains of RanBP2 with red/green opsin and the chaperone activity of these domains toward red/green opsin.
reports identification of a binding domain in RanBP2, the cyclophilin-like domain, toward components of the 19S cap of the proteasome
reports identification of a binding domain in RanBP2, the zinc-finger rich domain, toward CRM1/exportin-1
reports identification of a novel domain in RanBP2 located between RBD2 and RBD3 with specific binding activity against the conventional heavy chain kinesins, KIF5B and KIF5C
reports the novel subcellular localizations of RanBP2 in retinal neurons of human and bovine
the cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and protein biogenesis
RAN is a small GTP-binding protein of the RAS superfamily that is associated with the nuclear membrane and is thought to control a variety of cellular functions through its interactions with other proteins. This gene encodes a very large RAN-binding protein that immunolocalizes to the nuclear pore complex. The protein is a giant scaffold and mosaic cyclophilin-related nucleoporin implicated in the Ran-GTPase cycle. The encoded protein directly interacts with the E2 enzyme UBC9 and strongly enhances SUMO1 transfer from UBC9 to the SUMO1 target SP100. These findings place sumoylation at the cytoplasmic filaments of the nuclear pore complex and suggest that, for some substrates, modification and nuclear import are linked events. This gene is partially duplicated in a gene cluster that lies in a hot spot for recombination on chromosome 2q.
358 kDa nucleoporin
, E3 SUMO-protein ligase RanBP2
, nuclear pore complex protein Nup358
, nucleoporin 358
, nucleoporin Nup358
, ran-binding protein 2
, transformation-related protein 2
, RAN binding protein 2
, e3 SUMO-protein ligase RanBP2-like