Background:  Eukaryotic cells primarily utilize exoribonucleases and decapping enzymes to degrade their mRNA. DcpS is a scavenger pyrophosphatase that hydrolyzes the residual cap structure following 3' to 5' decay of an mRNA. Following mRNA degradation DcpS releases N-7 methyl guanosine monophosphate and 5'-diphosphate terminated cap or mRNA products. The central histidine within the DcpS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function. HIT proteins are homodimeric and contain two conserved 100-amino-acid HIT fold domains with independent active sites that are each sufficient to bind and hydrolyze cognate substrates. Necessary for the complete degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA fragments shorter than 10 nucleotides that are produced by 3'->5' exosome-mediated mRNA decay. Releases m7GMP. Can also degrade m7GDP to m7GMP. Has no activity towards mRNA molecules longer than 25 nucleotides.

Description: Rabbit polyclonal to DCPS

Immunogen: KLH conjugated synthetic peptide derived from DCPS

Specificity:  ·Reacts with Human, Mouse and Rat.

·Isotype: IgG

Application:  ·Western blotting: 1/100-500. Predicted Mol wt: 39 kDa;

·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;

·Immunocytochemistry/Immunofluorescence: 1/100;

·Immunoprecipitation: 1/50;

·ELISA: 1/500;

·Optimal working dilutions must be determined by the end user.