AARS1 antibody

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Description
AARS(alanyl-tRNA synthetase) is also named as AlaRS(alanine tRNA ligase 1, cytoplasmic), renal carcinoma antigen NY-REN-42 and belongs to the class-II aminoacyl-tRNA synthetase family. It can interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. AARS consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs(PMID:19661429).
Documents del producto
Product specifications
Category | Primary Antibodies |
Immunogen Target | alanyl-tRNA synthetase (AARS1) |
Host | Rabbit |
Reactivity | Human |
Recommended Dilution | WB: 1:200-1:1000; IHC: 1:20-1:200; IF: 1:20-1:200 |
Clonality | polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Observed MW | 107 kDa |
Purity | ≥95% as determined by SDS-PAGE |
Purification | Immunogen affinity purified |
Size 1 | 100µg |
Form | liquid |
Tested Applications | ELISA, WB, IHC, IF, IP |
Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.) |
UniProt ID | P49588 |
Alias | AARS1,AARS |
Background | Antibody anti-AARS1 |
Status | RUO |
Note | Mol. Weight 107 kDa |
Descripción
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AARS(alanyl-tRNA synthetase) is also named as AlaRS(alanine tRNA ligase 1, cytoplasmic), renal carcinoma antigen NY-REN-42 and belongs to the class-II aminoacyl-tRNA synthetase family. It can interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. AARS consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs(PMID:19661429).
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