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Ran/TC4-binding protein, RanBP1, interacts specifically with GTP-charged RAN. Additionally we are shipping RANBP1 Proteins (9) and many more products for this protein.
Showing 10 out of 70 products:
Human Monoclonal RANBP1 Primary Antibody for IF, WB - ABIN968158
Bischoff, Krebber, Smirnova, Dong, Ponstingl: Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1. in The EMBO journal 1995
Show all 3 Pubmed References
Human Polyclonal RANBP1 Primary Antibody for IHC, IHC (p) - ABIN256686
Štalekar, Yin, Rebolj, Darovic, Troakes, Mayr, Shaw, Rogelj: Proteomic analyses reveal that loss of TDP-43 affects RNA processing and intracellular transport. in Neuroscience 2015
Show all 2 Pubmed References
findings reveal an important mitotic role for RanBP1, controlling the spatial distribution and magnitude of mitotic Ran-GTP (show AK3 Antibodies) production and thereby ensuring accurate execution of Ran-dependent mitotic events
Sgk1 (show SGK1 Antibodies)-dependent regulation of RANBP1 has functional consequences on both mitotic microtubule activity and taxol sensitivity of cancer cells.
in vitro and in vivo phosphorylation of RanBP1 by Plk1 (show PLK1 Antibodies) as well as the importance of phosphorylation of RanBP1 in the interaction between Plk1 (show PLK1 Antibodies) and Ran during early mitosis, is demonstrated.
RANBP1 on 22q11.21 locus might be causally related to the smooth pursuit eye movement abnormality rather than the development of schizophrenia.
Downregulation of the Ran GTPase (show RAN Antibodies) effector RanBP1 is required for nuclear reorganisation.
structure of the Ran-RanBP1-RanGAP complex
Phosphorylated wild type RanGAP1 (show RANGAP1 Antibodies), but not a mutant harboring a mutation at the phosphorylation site 358S, efficiently formed a stable ternary complex with Ran and RanBP1 in vivo, suggesting that the 358S phosphorylation of RanGAP1 (show RANGAP1 Antibodies) affects the Ran system.
These data indicate that RANBP1 activity is required for the proper localization of specific factors that regulate microtubule function; loss of this activity contributes to the generation of aneuploidy in a microtubule-dependent manner.
RanBP1-interfered cells show an increased apoptotic response to taxol compared to their counterpart with normal or high RanBP1 levels, and this response is caspase-3 (show CASP3 Antibodies) dependent.
Generation of Ran-GTP (show AK3 Antibodies) from Ran-GDP by importin-beta (show KPNB1 Antibodies) is activated by Ran-binding protein-1 (RanBP1) that forms a trimeric complex with Ran-GDP and importin-beta (show KPNB1 Antibodies).
Ranbp1 emerges as a microcephaly gene within the 22q11.2 deleted region that may contribute to altered cortical precursor proliferation and neurogenesis associated with broader 22q11.2 deletion.
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.
The dramatic decrease in "RanBP" activity impairs germ cell viability and affects spermatogenesis decisively in RanBP1-knockout mice.
expressed in the frontonasal processes, branchial arches, aortic arches, and limb buds. At these sites, RanBP1 apparently coincides with neural crest-derived mesenchymal cells. In addition, RanBP1 is expressed in the forebrain
RanBP1 interferes with crucial factor(s) that control structural and dynamic features of centrosomes during mitosis
Tax (show CNTN2 Antibodies) directly binds Ran and Ran-binding protein-1, locates to centrosomes/spindle poles, and causes supernumerary centrosomes
Ran/TC4-binding protein, RanBP1, interacts specifically with GTP-charged RAN. RANBP1 encodes a 23-kD protein that binds to RAN complexed with GTP but not GDP. RANBP1 does not activate GTPase activity of RAN but does markedly increase GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). The RANBP1 cDNA encodes a 201-amino acid protein that is 92% similar to its mouse homolog. In both mammalian cells and in yeast, RANBP1 acts as a negative regulator of RCC1 by inhibiting RCC1-stimulated guanine nucleotide release from RAN.
RAN binding protein 1
, Ran binding protein 1
, ran binding protein 1
, ran-specific GTPase-activating protein
, HpaII tiny fragments locus 9A
, hpaII tiny fragments locus 9a protein
, ran-binding protein 1