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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) Antibodies (61) and Heterogeneous Nuclear Ribonucleoprotein U (Scaffold Attachment Factor A) Kits (27) and many more products for this protein.
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We found that heterogeneous nuclear ribonucleoprotein U (hnRNP U) is essential for the expression of Avp (show AVP Proteins) and Vip (show Vip Proteins). 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 Proteins), IL-6 (show IL6 Proteins) & IL-1beta (show IL1B Proteins). 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 Proteins) expression, binds the Oct4 (show POU5F1 Proteins) proximal promoter in ES cells, and dissociates from the promoter upon early differentiation induced by LIF (show LIF Proteins) withdrawal.
hnRNP-U engages a highly neddylated active SCF (show KITLG Proteins) beta-TrCP (show BTRC Proteins) 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 Proteins) gene with circadian timing
HnRNP U binding to the 5'-UTR of the Shh (show SHH Proteins) 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.
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 Proteins), ZBTB18 (show ZNF238 Proteins) and HNRNPU in humans
mutual regulatory mechanisms exist between PP4 (show ANXA5 Proteins) and SAF-A. Interactions between PP4 (show ANXA5 Proteins) and SAF-A played a role in prometaphase/metaphase transition.
CENP-W (show CENPW Proteins) interacts with hnRNPU and may contribute to kinetochore-microtubule attachment in mitotic cells.
Nuclear TDP-43 (show TARDBP Proteins) becomes neurotoxic by escaping from the inhibitory regulation by hnRNP-U or hnRNP (show HNRNPC Proteins)-A2. hnRNP-U inhibits TDP-43 (show TARDBP Proteins)-mediated alterations in splicing of POLDIP3 (show POLDIP3 Proteins) 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 and PP2A (show PPP2R4 Proteins), respectively, are required for accurate and timely exit from mitosis.
demonstrate that H19 inhibits RNA Pol II-mediated transcription by disrupting the hnRNP U-actin complex
Induction of caspase (show CASP3 Proteins)-9b expression is due to activation of hnRNP L (show HNRNPL Proteins) via phosphorylation to compete/inhibit hnRNP U association with exon 3 of Casp9 (show CASP9 Proteins) mRNA.
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