Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. Additionally we are shipping Phenylalanine-tRNA Synthetase 2 (Mitochondrial) Proteins (8) and many more products for this protein.
Showing 10 out of 32 products:
in patients with drug-resistant infantile spasm syndrome, associated with focal seizures, mild metabolic changes, and cerebral atrophy with volume loss of white matter on MRI (show C7ORF49 Antibodies), mutations in FARS2 should be considered.
Kinetic and structural changes in HsmtPheRS, induced by pathogenic mutations in human FARS2 have been described.
A newly identified missense mutation in FARS2 causes autosomal-recessive spastic paraplegia.
this study expands the phenotypic spectrum of FARS2 related disease and emphasizes intragenic deletion in the list of causative mutations.
the three FARS2 mutations directly impair aminoacylation function and stability of mtPheRS, leading to a decrease in overall tRNA charging capacity.
Two phenylalanyl-tRNA synthetase variants Ser57Cys and Asp280Ser both display wild-type aminoacylation activity and stability with respect to their free energies of unfolding, but are less stable at low hydrogen-ion concentration (pH).
Formation of the PheRS (show FARSA Antibodies)-tRNAPhe complex in human mitochondria must be accompanied by considerable rearrangement of the anticodon binding domain upon tRNA binding.
Mitochondrial and cytoplasmic phenylalanyl-tRNA synthetases (HsmtPheRS and HsctPheRS, respectively) catalyze direct attachment of m-Tyr (show TYR Antibodies) to tRNA(Phe).
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. This gene encodes 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.
, phenylalanine--tRNA ligase, mitochondrial
, phenylalanine-tRNA synthetase 1 (mitochondrial)
, phenylalanyl-tRNA synthetase, mitochondrial
, dJ236A3.1 (phenylalanine-tRNA synthetase)
, dJ520B18.2 (FARS1 (phenylalanine-tRNA synthetase))
, phenylalanine tRNA ligase 2, mitochondrial
, phenylalanine translase
, phenylalanine-tRNA synthetase 2 (mitochondrial)