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HNRNPU belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). Additionally we are shipping Heterogeneous Nuclear Ribonucleoprotein U (Scaffold Attachment Factor A) Kits (35) and Heterogeneous Nuclear Ribonucleoprotein U (Scaffold Attachment Factor A) Proteins (5) and many more products for this protein.
Showing 10 out of 65 products:
Mouse (Murine) Monoclonal HNRNPU Primary Antibody for ChIP, ELISA - ABIN108578
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 for ChIP, ELISA - ABIN108577
Ahmad, Lingrel: Kruppel-like factor 2 transcriptional regulation involves heterogeneous nuclear ribonucleoproteins and acetyltransferases. in Biochemistry 2005
Show all 8 Pubmed References
Mouse (Murine) Polyclonal HNRNPU Primary Antibody for 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
Show all 2 Pubmed References
Human Polyclonal HNRNPU Primary Antibody for 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 for 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 demonstrated that HNRNPU functions as a major factor maintaining 3D chromatin architecture, suggesting important roles of NM-associated proteins in genome organization.
We found that heterogeneous nuclear ribonucleoprotein U (hnRNP U) is essential for the expression of Avp (show AVP Antibodies) and Vip (show Vip Antibodies). 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 (show TNF Antibodies), IL-6 (show IL6 Antibodies) & IL-1beta (show IL1B Antibodies). 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 (show POU5F1 Antibodies) expression, binds the Oct4 (show POU5F1 Antibodies) proximal promoter in ES cells, and dissociates from the promoter upon early differentiation induced by LIF (show LIF Antibodies) withdrawal.
hnRNP-U engages a highly neddylated active SCF (show KITLG Antibodies) beta-TrCP (show BTRC Antibodies) 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 (show ARNTL Antibodies) gene with circadian timing
HnRNP U binding to the 5'-UTR (show UTS2R Antibodies) of the Shh (show SHH Antibodies) facilitates gene expression during limb development.
This series demonstrates common phenotypic features, including emerging dysmorphism, associated with heterozygous HNRNPU mutations. This allows us to define a novel neurodevelopmental syndrome, with a likely mechanism of haploinsufficiency
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 (show AKT3 Antibodies), ZBTB18 (show ZNF238 Antibodies) and HNRNPU in humans
mutual regulatory mechanisms exist between PP4 (show ANXA5 Antibodies) and SAF-A. Interactions between PP4 (show ANXA5 Antibodies) and SAF-A played a role in prometaphase/metaphase transition.
CENP-W (show CENPW Antibodies) interacts with hnRNPU and may contribute to kinetochore-microtubule attachment in mitotic cells.
Nuclear TDP-43 (show TARDBP Antibodies) becomes neurotoxic by escaping from the inhibitory regulation by hnRNP-U or hnRNP (show HNRNPC Antibodies)-A2. hnRNP-U inhibits TDP-43 (show TARDBP Antibodies)-mediated alterations in splicing of POLDIP3 (show POLDIP3 Antibodies) 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.
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