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SEP1 localizes to cytoplasmic foci containing a complex of mRNA-degrading enzymes. Additionally we are shipping XRN1 Antibodies (19) and XRN1 Proteins (3) and many more products for this protein.
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Data show that the AR-miR (show MLXIP ELISA Kits)-204-XRN1-miR (show MLXIP ELISA Kits)-34a positive feedback loop and a dual function of miR (show MLXIP ELISA Kits)-204/XRN1 axis in prostate cancer.
Thus, Xrn1 is a cellular factor regulating dsRNA accumulation and dsRNA-responsive innate immune effectors.
Occupation of each miR (show MLXIP ELISA Kits)-122 binding site on 5' untranslated region of the hepatitis C virus genome contributes equally and cooperatively to virus replication via protecting from Xrn1 exoribonuclease degradation.
Authors conclude that Xrn1 is the dominant 5' exoribonuclease mediating decay of hepatitis C virus RNA and that miR (show MLXIP ELISA Kits)-122 provides protection against it
Mouse Xrn1 plays a role in RNA turnover.
Data show that 5' exonuclease (show EXO1 ELISA Kits) Xrn1 knockdown and miR (show MLXIP ELISA Kits)-122 supplementation have equal, redundant, and nonadditive effects on the rate of viral RNA decay, indicating that miR (show MLXIP ELISA Kits)-122 protects HCV RNA from 5' decay.
findings reveal a role for XRN1 in decapping and provide a molecular basis for the coupling of decapping to 5'-->3' mRNA degrada
LSm1 (show LSM1 ELISA Kits)-7 proteins colocalize with DCP1 (show ACE ELISA Kits),DCP2 (show DCP2 ELISA Kits) and Xrn1 in cytoplasmic foci
XRN1 knockdown impairs the translational repression triggered by NMDA. Collectively, these observations support a role for the SX-bodies in the reversible masking and silencing of mRNAs at the synapse.
SEP1 localizes to cytoplasmic foci containing a complex of mRNA-degrading enzymes. In addition to mRNA metabolism, yeast Sep1 has been implicated in a variety of nuclear and cytoplasmic functions, including homologous recombination, meiosis, telomere maintenance, and microtubule assembly.
5'-3' exoribonuclease 1
, strand-exchange protein 1 homolog
, protein Dhm2