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HPA018148

Sigma-Aldrich

Anti-FARS2 antibody produced in rabbit

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Sinónimos:

Anti-PheRS, Anti-Phenylalanine--tRNA ligase, Anti-Phenylalanyl-tRNA synthetase, mitochondrial precursor

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About This Item

UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.43

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

product line

Prestige Antibodies® Powered by Atlas Antibodies

form

buffered aqueous glycerol solution

species reactivity

human

enhanced validation

recombinant expression
Learn more about Antibody Enhanced Validation

technique(s)

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:20-1:50

immunogen sequence

GTPLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYRRDQIDSQHYPIFHQLEAVRLFSKHELFAGIKDGES

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... FARS2(10667)

General description

The gene Phenylalanyl-tRNA synthetase (FARS2) has been mapped to human chromosome 6p25.1. Three isoforms of phenylalanyl-tRNA synthase exist: the bacterial (αβ)2 heterodimer, the archaeal/eukaryotic cytosolic (αβ)2 heterodimer and the mitochondrial monomer. The human mitochondrial phenylalanyl-tRNA synthetase (FARS2) consists of a single polypeptide chain and is the smallest known nuclear-encoded synthetase. The protein has four major domains: an N-terminal region, a catalytic domain, a linker region and a C-terminal domain.

Immunogen

Phenylalanyl-tRNA synthetase, mitochondrial precursor recombinant protein epitope signature tag (PrEST)

Application

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.

Biochem/physiol Actions

The aminoacyl-tRNA synthetases are responsible for catalyzing the attachment of the correct amino acid to its related tRNA. Phenylalanyl-tRNA synthetase (FARS2) could also catalyze binding of oxidized phenylalanine, meta-tyrosine, to the tRNAPhe. This causes transfer of the misacylated tRNA to the ribosome and addition of ROS-damaged amino acid into eukaryotic proteins. Humans with heterozygous mutations in FARS2 (I329T, D391V, Y144C) suffer from fatal epileptic mitochondrial encephalopathy. FARS2 mutations impair the aminoacylation function and stability of the protein, leading to decrease in tRNA charging capacity. Additionally, missense mutation in FARS2 (D325Y) causes mitochondrial disease phenotype associated with respiratory chain dysfunction (respiratory chain complex IV deficiency in muscle) and early-onset epilepsy.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Linkage

Corresponding Antigen APREST72521

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificados de análisis (COA)

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J M Bullard et al.
Journal of molecular biology, 288(4), 567-577 (1999-05-18)
Human mitochondrial phenylalanyl-tRNA synthetase (mtPheRS) has been identified from the human EST database. Using consensus sequences derived from conserved regions of the alpha and beta-subunits from bacterial PheRS, two partially sequenced cDNA clones were identified. Unexpectedly, sequence analysis indicated that
Abdulraheem Almalki et al.
Biochimica et biophysica acta, 1842(1), 56-64 (2013-10-29)
Mitochondrial aminoacyl-tRNA synthetases (aaRSs) are essential enzymes in protein synthesis since they charge tRNAs with their cognate amino acids. Mutations in the genes encoding mitochondrial aaRSs have been associated with a wide spectrum of human mitochondrial diseases. Here we report
Jenni M Elo et al.
Human molecular genetics, 21(20), 4521-4529 (2012-07-27)
Next-generation sequencing has turned out to be a powerful tool to uncover genetic basis of childhood mitochondrial disorders. We utilized whole-exome analysis and discovered novel compound heterozygous mutations in FARS2 (mitochondrial phenylalanyl transfer RNA synthetase), encoding the mitochondrial phenylalanyl transfer
Liron Klipcan et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(27), 11045-11048 (2009-06-25)
The accumulation of proteins damaged by reactive oxygen species (ROS), conventionally regarded as having pathological potentials, is associated with age-related diseases such as Alzheimer's, atherosclerosis, and cataractogenesis. Exposure of the aromatic amino acid phenylalanine to ROS-generating systems produces multiple isomers

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