Decapping and exoribonuclease protein (DXO), human, recombinant

Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 1-396aa. Protein Length: Full Length. Tag Info: C-terminal 6xHis-tagged. Target Protein Sequence: MDPRGTKRGA EKTEVAEPRN KLPRPAPSLP TDPALYSGPF PFYRRPSELG CFSLDAQRQY HGDARALRYY SPPPTNGPGP NFDLRDGYPD RYQPRDEEVQ ERLDHLLCWL LEHRGRLEGG PGWLAEAIVT WRGHLTKLLT TPYERQEGWQ LAASRFQGTL YLSEVETPNA RAQRLARPPL LRELMYMGYK FEQYMCADKP GSSPDPSGEV NTNVAFCSVL RSRLGSHPLL FSGEVDCTDP QAPSTQPPTC YVELKTSKEM HSPGQWRSFY RHKLLKWWAQ SFLPGVPNVV AGFRNPDGFV SSLKTFPTMK MFEYVRNDRD GWNPSVCMNF CAAFLSFAQS TVVQDDPRLV HLFSWEPGGP VTVSVHQDAP YAFLPIWYVE AMTQDLPSPP KTPSPK. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: n/a. Biological Activity: Not Test. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA. The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay. Preferentially acts on NAD-capped transcripts in response to environmental stress. Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation. Specifically degrades pre-mRNAs with a defective 5'-end m7G cap and is part of a pre-mRNA capping quality control. Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1). In contrast to canonical decapping enzymes DCP2 and NUDT16, which cleave the cap within the triphosphate linkage, the decapping activity releases the entire cap structure GpppN and a 5'-end monophosphate RNA. Also has 5'-3' exoribonuclease activities: The 5'-end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs. Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates. Exhibits decapping activity towards FAD-capped RNAs. Exhibits decapping activity towards dpCoA-capped RNAs in vitro. Reference: n/a. Function: nan