Recombinant Xenopus Laevis Decapping And Exoribonuclease Protein (DXO) Protein (His)

Name: Recombinant Xenopus Laevis Decapping And Exoribonuclease Protein (DXO) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00117P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins, Recombinant proteins fall special offers - full-length proteins

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Product Overview

Description	Recombinant Xenopus Laevis Decapping And Exoribonuclease Protein (DXO) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	Q5HZT0
Target Symbol	DXO
Synonyms	(DXO)(5'-3' exoribonuclease DXO)(Dom-3 homolog Z)(NAD-capped RNA hydrolase DXO)(DeNADding enzyme DXO)
Species	Xenopus laevis (African clawed frog)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MEGNKSMQREKIDRPMKRGPEQNSLSPPLAKCPFMSCSSLKTLHSLYQGSFPFYRLPSEVGHFSLDENRQYHQDNRKLRYYSPPVGIREKGSPGWNVMDGYESHYVRRNEDEKEGLLHILTWLEKNRGVLGAHVEGGSKRPIDRDFVTWRGHLTKILCTPYETQEGWLLAVTLFKGTFYISEQETEAAQKKRKERSLEQERLMYSGYKFESYICADSPDRQPSQSAVVNTNEGFCSVLLARLTSHSLLISGEVDCTDPSAKKSIPPTCYIELKSSAQIRNPHQQRSFNRYKLLKWWCQSFLLGIPIIVAGFRSPEGRIVSLETFKTSDIPHLVRGERNSWDPAVCMNFCNKFLSHIKSVVTRDDPRLVYLFAWEPGCDVTFTVHTDPEYTILPSWYVNSVN
Expression Range	1-401aa
Protein Length	Full Length
Mol. Weight	50.3 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target Function	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. 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). 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.
Subcellular Location	Nucleus.
Protein Families	DXO/Dom3Z family
Database References	KEGG: xla:496313 UniGene: Xl.3904

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.