Thermo Fisher Scientific FARS2 Polyclonal Antibody

Applications

Tested Dilution

Publications

Western Blot (WB)

0.5-2 µg/mL

-

Immunohistochemistry (Paraffin) (IHC (P))

5-20 µg/mL

-

Immunocytochemistry (ICC/IF)

5-20 µg/mL

-

Product Specifications

Species Reactivity

Rat

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

Recombinant protein Phenylalanyl tRNA Synthetase 2, Mitochondrial. The antigen corresponds to amino acid range 1-472 of the target protein. if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:FARS2,uniProtId:Q6AYQ3-1,ncbiNodeId:10114,antigenRange:1-472,antigenLength:472,antigenImageFileName:PA5-119336_FARS2_Q6AYQ3-1_Rabbit.svg,antigenImageFileNamePDP:PA5-119336_FARS2_Q6AYQ3-1_Rabbit_PDP.jpeg,sortOrder:2}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

View immunogen .st0{fill:#FFFFFF;} .st1{fill:#1E8AE7;}

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

0.51 mg/mL

Purification

Antigen affinity chromatography

Storage buffer

PBS with 50% glycerol

Contains

0.05% ProClin 300

Storage conditions

-20°C

Shipping conditions

Wet ice

RRID

AB_2903834

Target Information

Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. FARS2 is a phenylalanine-tRNA synthetase (PheRS) localized to the mitochondrion which consists of a single polypeptide chain, unlike the (alpha-beta)2 structure of the prokaryotic and eukaryotic cytoplasmic forms of PheRS. Structure analysis and catalytic properties indicate mitochondrial PheRSs may constitute a class of PheRS distinct from the enzymes found in prokaryotes and in the eukaryotic cytoplasm. Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. FARS1 encodes a mitochondrially-located phenylalanine-tRNA synthetase (PheRS) which consists of a single polypeptide chain unlike the (alpha-beta)2 structure of the prokaryotic and eukaryotic cytoplasmic forms of PheRS. Structure analysis and catalytic properties indicate mitochondrial PheRSs may constitute a class of PheRS distinct from the enzymes found in prokaryotes and the eukaryotic cytoplasm.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.