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The protein encoded by NUDT21 is one subunit of a cleavage factor required for 3' RNA cleavage and polyadenylation processing. Additionally we are shipping Nudix (Nucleoside Diphosphate Linked Moiety X)-Type Motif 21 Proteins (12) and Nudix (Nucleoside Diphosphate Linked Moiety X)-Type Motif 21 Kits (7) and many more products for this protein.
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Findings suggest that CFIm25 plays an important role in lung cancer cell proliferation through regulating the alternative polyadenylation (APA) of oncogenes.
RNA sequence preferences of unconventional RNA-binding proteins, Nudt21 and CNBP, has been described.
Loss of NUDT21 shortened the 3'-UTR of various oncogenes in hepatocellular carcinoma cells. The shorter 3'-UTR contained less miRNA binding sites, which enabled the oncogenes to evade miRNA regulation and become overexpressed in HCC, leading to unregulated cancer cell proliferation.
it was demonstrated that the CFIm25 protein was also downregulated in osteosarcoma tissues, and inhibited the proliferation and promoted the apoptosis of the cells. Elucidating the roles of miR181a and CFIm25 in osteosarcoma not only assists in further understanding the pathogenesis and progression of this disease, but also offers novel targets for effective therapies.
The authors identify NUDT21 as a novel candidate for intellectual disability and neuropsychiatric disease, and elucidate a mechanism of pathogenesis by MeCP2 dysregulation via altered alternative polyadenylation.
Crystal structure of CFIm25-CFIm68 RRM heterotetramer illustrated that CFIm25 homodimer is clamped by two CFIm68 monomers on each side of the dimer interface.
Data provide evidence that CFIm exists as a heterotetramer of 25-kD, 59-kD and 68-kD subunits of CFIm: CFIm25, CFIm59 and CFIm68.
crystal structures of the CFI(m)25 homodimer in complex with UGUAAA and UUGUAU RNA sequences
region in the subunit of CF I(m) involved in RNA binding, protein-protein interactions, and subcellular localization
Evidence that CFIm25 regulates alternative poly(A) site selection of genes with tandem poly(A) signals in their 3'-UTRs.
Results from crystallographic and biochemical experiments suggest that CF I(m)25 makes use of its Nudix fold to bind but not hydrolyze ATP and diadenosine tetraphosphate.
The crystal structure of human CPSF5 was solved at 1.9 A resolution.
Here we report that the CFIm subunits NUDT21/CPSF5 and CPSF6 are highly enriched in mouse male germ cells relative to somatic cells.
The protein encoded by this gene is one subunit of a cleavage factor required for 3' RNA cleavage and polyadenylation processing. The interaction of the protein with the RNA is one of the earliest steps in the assembly of the 3' end processing complex and facilitates the recruitment of other processing factors. This gene encodes the 25kD subunit of the protein complex, which is composed of four polypeptides.
CPSF 25 kDa subunit
, cleavage and polyadenylation specific factor 5, 25 kD subunit
, cleavage and polyadenylation specific factor 5, 25 kDa
, cleavage and polyadenylation specificity factor 25 kDa subunit
, cleavage and polyadenylation specificity factor subunit 5
, cleavage factor Im complex 25 kDa subunit
, nucleoside diphosphate-linked moiety X motif 21
, nudix motif 21
, pre-mRNA cleavage factor Im (25kD)
, pre-mRNA cleavage factor Im 25 kDa subunit
, pre-mRNA cleavage factor Im, 25kD subunit
, cleavage and polyadenylation specific factor 5
, Cleavage and polyadenylation specificity factor 5
, cleavage and polyadenylation specificity factor subunit 5-like