FARS2 Rabbit Polyclonal Antibody

CAT#: TA356108

FARS2 Antibody - N-terminal region

Product Images

WB Suggested Anti-FARS2 Antibody Titration: 5.0ug/ml ELISA Titer: 1:62500 Positive Control: Transfected 293T

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  Rabbit Anti-FARS2 Antibody Catalog Number: ARP40669 Paraffin Embedded Tissue: Human Muscle Cellular Data: Skeletal muscle cells Antibody Concentration: 4.0-8.0 ug/ml Magnification: 400X

Specifications

Product Data

• Applications: IHC, WB
• Reactivities: Human
• Host: Rabbit
• Clonality: Polyclonal
• Immunogen: The immunogen is a synthetic peptide directed towards the N terminal region of human FARS2
• Specificity: Expected reactivity: Cow, Dog, Guinea Pig, Horse, Human, Mouse, Rabbit, Rat
  Homology: Cow: 93%; Dog: 92%; Guinea Pig: 85%; Horse: 83%; Human: 100%; Mouse: 92%; Rabbit: 100%; Rat: 93%
• Formulation: Liquid. Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
• Concentration: lot specific
• Purification: Protein A purified
• Conjugation: Unconjugated
• Storage: For short term use, store at 2-8°C up to 1 week. For long term storage, store at -20°C in small aliquots to prevent freeze-thaw cycles.
• Predicted Protein Size: 50kDa
• Gene Name: phenylalanyl-tRNA synthetase 2, mitochondrial
• Database Link:
  NP_006558
  Entrez Gene 10667 Human
  UniProt ID O95363
• Background: 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.
• Synonyms: dJ236A3.1; dJ520B18.2; FARS1; HSPC320; OTTHUMP00000015986; PheRS

Reference Data

• Protein Pathways: Aminoacyl-tRNA biosynthesis