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HNRNPU belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). Zusätzlich bieten wir Ihnen Heterogeneous Nuclear Ribonucleoprotein U (Scaffold Attachment Factor A) Kits (27) und Heterogeneous Nuclear Ribonucleoprotein U (Scaffold Attachment Factor A) Proteine (4) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 59 products:
Mouse (Murine) Monoclonal HNRNPU Primary Antibody für ChIP, ELISA - ABIN108577
Dreyfuss, Choi, Adam: Characterization of heterogeneous nuclear RNA-protein complexes in vivo with monoclonal antibodies. in Molecular and cellular biology 1984
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Mouse (Murine) Monoclonal HNRNPU Primary Antibody für ChIP, ELISA - ABIN108578
Ahmad, Lingrel: Kruppel-like factor 2 transcriptional regulation involves heterogeneous nuclear ribonucleoproteins and acetyltransferases. in Biochemistry 2005
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Chicken Monoclonal HNRNPU Primary Antibody für IF, IP - ABIN967770
Eger, Stockinger, Schaffhauser, Beug, Foisner: Epithelial mesenchymal transition by c-Fos estrogen receptor activation involves nuclear translocation of beta-catenin and upregulation of beta-catenin/lymphoid enhancer binding factor-1 transcriptional activity. in The Journal of cell biology 2000
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Mouse (Murine) Polyclonal HNRNPU Primary Antibody für IC, IF - ABIN2452032
Kiledjian, Dreyfuss: Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box. in The EMBO journal 1992
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Human Polyclonal HNRNPU Primary Antibody für IHC (p), IHC - ABIN151573
Banerjee, Mandal, Das, Hegde, Das, Bhakat, Boldogh, Sarkar, Mitra, Hazra: Preferential repair of oxidized base damage in the transcribed genes of mammalian cells. in The Journal of biological chemistry 2011
Human Polyclonal HNRNPU Primary Antibody für IP, WB - ABIN151574
Powell, Coulson, Crary, Wong, Ach, Tsang, Alice Yamada, Yasui, Lasalle: A Prader-Willi locus lncRNA cloud modulates diurnal genes and energy expenditure. in Human molecular genetics 2013
We found that heterogeneous nuclear ribonucleoprotein U (hnRNP U) is essential for the expression of Avp (zeige AVP Antikörper) and Vip (zeige Vip Antikörper). Loss of one copy of the Hnrnpu gene resulted in fragmented locomotor activities and disrupted metabolic rhythms. Hnrnpu(+/-) mice were more active than wild-type mice in the daytime but more inactive at night.
findings provide conclusive evidence for the essential role of hnRNP U in heart development and function and in the regulation of alternative splicing.
SAF-A interacts with BRG1 and both components are required for RNA Polymerase II Mediated Transcription
Macrophage expression of hnRNP U was induced by TLR stimulation. hnRNP U knockdown attenuated & overexpression increased TLR-induced expression of TNF-alpha (zeige TNF Antikörper), IL-6 (zeige IL6 Antikörper) & IL-1beta (zeige IL1B Antikörper). hnRNP U bound to the mRNA of these cytokines via the RGG motif.
Data report that endogenous SAF-A is involved in regulation of Oct4 (zeige POU5F1 Antikörper) expression, binds the Oct4 (zeige POU5F1 Antikörper) proximal promoter in ES cells, and dissociates from the promoter upon early differentiation induced by LIF (zeige LIF Antikörper) withdrawal.
hnRNP-U engages a highly neddylated active SCF (zeige KITLG Antikörper) beta-TrCP (zeige BTRC Antikörper) which dissociates in the presence of a high-affinity substrate, resulting in the ubiquitination of the latter.
hnRNP U participates in nuclear regulatory events that are involved in mammalian central and peripheral circadian clocks.
nuclear matrix protein SAF-A binds to the 3'-flanking region of the Bmal1 (zeige ARNTL Antikörper) gene with circadian timing
HnRNP U binding to the 5'-UTR (zeige UTS2R Antikörper) of the Shh (zeige SHH Antikörper) facilitates gene expression during limb development.
SAF-A was found to be localized in three different domains: outside the chromosomes, on the surface of the chromosome arms, and in the centromere region where it apparently binds specifically to the satellite DNA.
SAF-A, in concert with Ku, temporally regulates base damage repair in irradiated cell genome.
HNRPU deletion is associated with neurodevelopmental disorders.
We broaden the clinical and mutational HNRNPU-associated spectrum, and demonstrate that heterozygous HNRNPU variants cause epilepsy, severe intellectual disability with striking speech impairment and variable central nervous system, cardiac, and renal anomalies.
Results show that SAF-A and caRNAs form a dynamic, transcriptionally responsive chromatin mesh that organizes large-scale chromosome structures and protects the genome from instability.
results confirm and refine the complex genotype-phenotype correlations existing in the 1qter microdeletion syndrome and define more precisely the neurodevelopmental phenotypes associated with genetic alterations of AKT3 (zeige AKT3 Antikörper), ZBTB18 (zeige ZNF238 Antikörper) and HNRNPU in humans
mutual regulatory mechanisms exist between PP4 (zeige ANXA5 Antikörper) and SAF-A. Interactions between PP4 (zeige ANXA5 Antikörper) and SAF-A played a role in prometaphase/metaphase transition.
CENP-W (zeige CENPW Antikörper) interacts with hnRNPU and may contribute to kinetochore-microtubule attachment in mitotic cells.
Nuclear TDP-43 (zeige TARDBP Antikörper) becomes neurotoxic by escaping from the inhibitory regulation by hnRNP-U or hnRNP (zeige HNRNPC Antikörper)-A2. hnRNP-U inhibits TDP-43 (zeige TARDBP Antikörper)-mediated alterations in splicing of POLDIP3 (zeige POLDIP3 Antikörper) mRNA.
These results suggest that HNRNPU, FAM36A, and NCRNA00201 are not major genes for microcephaly and corpus callosum abnormalities but are good candidates for intellectual disability (ID) and seizures.
both phosphorylation and dephosphorylation of SAF-A serine 59 by PLK1 (zeige PLK1 Antikörper) and PP2A (zeige PPP2R4 Antikörper), respectively, are required for accurate and timely exit from mitosis.
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they form complexes with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene contains a RNA binding domain and scaffold-associated region (SAR)-specific bipartite DNA-binding domain. This protein is also thought to be involved in the packaging of hnRNA into large ribonucleoprotein complexes. During apoptosis, this protein is cleaved in a caspase-dependent way. Cleavage occurs at the SALD site, resulting in a loss of DNA-binding activity and a concomitant detachment of this protein from nuclear structural sites. But this cleavage does not affect the function of the encoded protein in RNA metabolism. At least two alternatively spliced transcript variants have been identified for this gene.
, heterogenous nuclear ribonucleoprotein U
, nuclear matrix protein sp120
, scaffold attachment factor A
, system N1 Na+ and H+-coupled glutamine transporter
, transporter protein
, transporter protein; system N1 Na+ and H+-coupled glutamine transporter
, heterogeneous nuclear ribonucleoprotein U
, p120 nuclear protein