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Mouse (Murine) Monoclonal RANGAP1 Primary Antibody für ICC, IF - ABIN1042672
Xia, Lee, Altieri: Tumor cell dependence on Ran-GTP-directed mitosis. in Cancer research 2008
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Human Polyclonal RANGAP1 Primary Antibody für IHC (p), IHC - ABIN250151
Bischoff, Krebber, Kempf, Hermes, Ponstingl: Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport. in Proceedings of the National Academy of Sciences of the United States of America 1995
Cow (Bovine) Polyclonal RANGAP1 Primary Antibody für WB - ABIN2786743
Ewing, Chu, Elisma, Li, Taylor, Climie, McBroom-Cerajewski, Robinson, OConnor, Li, Taylor, Dharsee, Ho, Heilbut, Moore, Zhang, Ornatsky, Bukhman, Ethier, Sheng, Vasilescu, Abu-Farha, Lambert, Duewel et al.: Large-scale mapping of human protein-protein interactions by mass spectrometry. ... in Molecular systems biology 2007
NUSAP1 (zeige NUSAP1 Antikörper) contributes to accurate chromosome segregation by acting as a co-factor for RanBP2 (zeige RANBP2 Antikörper)-RanGAP1-UBC9 (zeige UBE2I Antikörper) during cell division.
RanGAP1 upregulation is associated with drug resistance in Chronic Myeloid Leukemia (zeige BCL11A Antikörper).
Abnormal localization of RanGAP1 was found in cortex of Huntington's disease patients.
our results elucidate that RanGAP1 is actively transported between the nuclear and cytoplasmic compartments, and that the cytoplasmic and NPC (zeige NPC1 Antikörper) localization of RanGAP1 is dependent on CRM1 (zeige XPO1 Antikörper)-mediated nuclear export.
immune cell adaptor SLP-76 (zeige LCP2 Antikörper) binds directly to SUMO-RanGAP1 of cytoplasmic fibrils of the nuclear pore complex, and this interaction is needed for optimal NFATc1 (zeige NFATC1 Antikörper) and NF-kappaB (zeige NFKB1 Antikörper) p65 (zeige GORASP1 Antikörper) nuclear entry in T cells
Differentiation of human coronary artery smooth muscle cell to a contractile phenotype by stepwise serum depletion leads to significant reduction of RanGAP1 protein levels.
Determinants of small ubiquitin-like modifier 1 (SUMO1 (zeige SUMO1 Antikörper)) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin (zeige AGFG2 Antikörper) RanBP2 (zeige RANBP2 Antikörper).
Analysis of the dynamics of E2(Ubc9 (zeige UBE2I Antikörper))-SUMO-Target(RanGAP1) in the absence and presence of E3(RanBP2 (zeige RANBP2 Antikörper)) revealed that two different allosteric sites regulate the ligase activity.
the RanGAP1 consensus sumoylation site and SUMO-1 (zeige SUMO1 Antikörper) C terminus are both conformationally flexible
the 3.0-A crystal structure of a four-protein complex of Ubc9 (zeige UBE2I Antikörper), a Nup358/RanBP2 (zeige RANBP2 Antikörper) E3 ligase domain (IR1 (zeige NISCH Antikörper)-M) and SUMO-1 (zeige SUMO1 Antikörper) conjugated to the carboxy-terminal domain of RanGAP1
data suggest that remodeling of the RanGAP-mediated nuclear transport system plays a key role in cell cycle exit for terminal differentiation of cortical neurons
nuclear localization of Ran was strongly increased in MYCBP2 (zeige MYCBP2 Antikörper)-deficient DRGs
immune cell adaptor SLP-76 (zeige LCP2 Antikörper) binds directly to SUMO-RanGAP1 of cytoplasmic fibrils of the nuclear pore complex, and this interaction is needed for optimal NFATc1 (zeige NFATC1 Antikörper) and NF-kappaB (zeige NFKB1 Antikörper) p65 (zeige NFkBP65 Antikörper) nuclear entry in T cells
These data suggest a dual function of the Nup358 (zeige RANBP2 Antikörper)-RanGAP1 complex as a coordinator of importin beta (zeige KPNB1 Antikörper) recycling and reformation of novel import complexes.
Protection from isopeptidase-mediated deconjugation regulates paralog-selective sumoylation of RanGAP1.
The data show that plant development is differentially affected by RanGAP mutant allele combinations of increasing severity and requires the GAP activity of RanGAP, while the subcellular positioning of RanGAP is dispensable.
AtRanGAP1 has a mitotic trafficking pattern uniquely different from that of vertebrate RanGAP.
In a wip1-1/wip2-1/wip3-1 triple mutant, RanGAP1 is dislocated from the nuclear envelope in undifferentiated root-tip cells, whereas nuclear envelope targeting in differentiated root cells and targeting to the cell plate remain intact.
Data suggest that an unanticipated complexity of RanGAP nuclear envelope targeting and at least one member of each NE-associated coiled-coil and transmembrane domains protein family is required for RanGAP targeting in root tip cells.
propose that Arabidopsis RanGAP, a continuous positive protein marker of the plant division plane, has a role in spatial signaling during plant cell division
These data suggest that both HSC70-1 and the WPP-domain proteins play a role in facilitating WIT1 nuclear envelope targeting; this may be the first described in planta activity for the WPP-domain proteins.
RanGAP1, is a homodimeric 65-kD polypeptide that specifically induces the GTPase activity of RAN, but not of RAS by over 1,000-fold. RanGAP1 is the immediate antagonist of RCC1, a regulator molecule that keeps RAN in the active, GTP-bound state. The RANGAP1 gene encodes a 587-amino acid polypeptide. The sequence is unrelated to that of GTPase activators for other RAS-related proteins, but is 88% identical to Fug1, the murine homolog of yeast Rna1p. RanGAP1 and RCC1 control RAN-dependent transport between the nucleus and cytoplasm. RanGAP1 is a key regulator of the RAN GTP/GDP cycle.
ran GTPase-activating protein 1
, segregation distorter homolog
, segregation distortion
, ran GTPase activating protein 1
, Ran GTPase activating protein 1 b
, Ran GTPase activating protein 1
, RAN GTPase activating protein 1
, RAN GTPase activating protein 1 a
, CG9999 gene product from transcript CG9999-RA
, Protein segregation distorter
, Ran-GTPase activating protein
, segregation distorter