Recombinant Human AARS, GST-tagged

• Cat.No.: AARS-9196H
• Product Overview: Recombinant human AARS protein, fused to GST-tag, was expressed in E.coli and purified by GST-sepharose.

Specification

• Species: Human
• Source: E.coli
• Tag: GST
• Protein Length: 1-350a.a.
• Description: The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. Class II tRNA synthases evolved early in evolution and are highly conserved. This is reflected by the fact that 498 of the 968-residue polypeptide human AARS shares 41% identity witht the E.coli protein. tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. They consist of a catalytic domain which interacts with the amino acid acceptor-T psi C helix of the tRNA, and a second domain which interacts with the rest of the tRNA structure.
• Storage: The protein is stored in PBS buffer at -20℃. Avoid repeated freezing and thawing cycles.
• Storage Buffer: 1M PBS (58mM Na2HPO4,17mM NaH2PO4, 68mM NaCl, pH8. ) added with 100mM GSH and 1% Triton X-100,15%glycerol.

Gene Information

• Gene Name: AARS alanyl-tRNA synthetase [ Homo sapiens ]
• Official Symbol: AARS
• Synonyms: AARS; alanyl-tRNA synthetase; alanine--tRNA ligase, cytoplasmic; alanine tRNA ligase 1; cytoplasmic; alaRS; renal carcinoma antigen NY-REN-42; alanine tRNA ligase 1, cytoplasmic; alanyl-tRNA synthetase, cytoplasmic; CMT2N
• Gene ID: 16
• mRNA Refseq: NM_001605
• Protein Refseq: NP_001596
• MIM: 601065
• UniProt ID: P49588
• Chromosome Location: 16q22
• Pathway: Aminoacyl-tRNA biosynthesis, organism-specific biosystem; Aminoacyl-tRNA biosynthesis, conserved biosystem; Aminoacyl-tRNA biosynthesis, eukaryotes, organism-specific biosystem; Aminoacyl-tRNA biosynthesis, eukaryotes, conserved biosystem; Cytosolic tRNA aminoacylation, organism-specific biosystem; Gene Expression, organism-specific biosystem; tRNA Aminoacylation, organism-specific biosystem
• Function: ATP binding; alanine-tRNA ligase activity; amino acid binding; aminoacyl-tRNA editing activity; ligase activity; metal ion binding; nucleotide binding; tRNA binding