Dtd2 (NM_029545) Mouse Recombinant Protein

CAT#: TP520756

Purified recombinant protein of Mouse D-tyrosyl-tRNA deacylase 2 (Dtd2), with C-terminal MYC/DDK tag, expressed in HEK293T cells, 20ug

Specifications

Product Data

• Species: Mouse
• Expression Host: HEK293T
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  >MR220756 protein sequence
  Red=Cloning site Green=Tags(s)
  
  MADGGRVAQARALLQQCLHARLQVRPADGDAAAQWVEIRRGLVIYVCFFKGADTDLLPKMVNTLLNVKLS
  ETETGKHVSILDLPGDVLIIPQATLGGRVKGRSMQYHSNSGKEEGSELYSQFVSLCEKAVANNTKSVEAG
  VAVAHGTYGNRQVLKLDTNGPYTHLIEF
  
  TRTRPLEQKLISEEDLAANDILDYKDDDDKV
• Tag: C-MYC/DDK
• Predicted MW: 18.2 kDa
• Concentration: >0.05 µg/µL as determined by microplate BCA method
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Buffer: 25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol
• Note: For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process.
• Storage: Store at -80°C after receiving vials.
• Stability: Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.

Reference Data

• RefSeq: NP_083821
• Locus ID: 328092
• UniProt ID: Q8BHA3
• Cytogenetics: 12 C1
• Refseq Size: 2564
• Refseq ORF: 507
• Synonyms: 4930578F06Rik; 6530401N04Rik; B830049N13Rik
• Summary: Deacylates mischarged D-aminoacyl-tRNAs. Probably acts by rejecting L-amino acids from its binding site rather than specific recognition of D-amino acids. Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl-tRNA(Tyr). By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality. In contrast to DTD1, deacylates L-Ala mischarged on tRNA(Thr)(G4.U69) by alanine-tRNA ligase AARS. Can deacylate L-Ala due to a relaxed specificity for substrate chirality caused by the trans conformation of the Gly-Pro motif in the active site. Also hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly) in vitro, although in vivo EEF1A1/EF-Tu may protect cognate achiral glycyl-tRNA(Gly) from DTD2-mediated deacetylation.[UniProtKB/Swiss-Prot Function]