HPA002383

Sigma-Aldrich

Anti-CARS antibody produced in rabbit

enhanced validation

Ab1, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):
Anti-Cysteine--tRNA ligase antibody produced in rabbit, Anti-CysRS antibody produced in rabbit, Anti-Cysteinyl-tRNA synthetase, cytoplasmic antibody produced in rabbit
Human Protein Atlas Number:

biological source

rabbit

Quality Level

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

rat, mouse, human

packaging

antibody small pack of 25 μL

enhanced validation

independent
orthogonal RNAseq
Learn more about Antibody Enhanced Validation

application(s)

immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:50-1:200

immunogen sequence

SQCNLYMAARKAVRKRPNQALLENIALYLTHMLKIFGAVEEDSSLGFPVGGPGTSLSLEATVMPYLQVLSEFREGVRKIAREQKVPEILQLSDALRDNILPELGVRFEDHEGLPTVVKLVDRNTLLKEREEKRRVE

conjugate

unconjugated

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... CARS(833)

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Immunogen

Cysteinyl-tRNA synthetase, cytoplasmic recombinant protein epitope signature tag (PrEST)

Biochem/physiol Actions

In human, CARS (cysteinyl-tRNA synthetase) protein comprises of a nucleotide-binding fold region that constitutes the potential active site and class I signature motifs, HIGH and KMSKS, in the catalytic domain. It plays a crucial role in aminoacylation of human cytoplasmic tRNA(Cys) with cysteine. It accelerates the addition of cysteine to its cognate tRNA.

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 APREST86199.

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 Sigma-Aldrich Co. LLC

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

RIDADR

NONH for all modes of transport

WGK Germany

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

E Davidson et al.
Biological chemistry, 382(3), 399-406 (2001-05-12)
Cysteinyl-tRNA synthetase catalyzes the addition of cysteine to its cognate tRNA. The available eukaryotic sequences for this enzyme contain several insertions that are absent from bacterial sequences. To gain insights into the differences between the bacterial and eukaryotic forms, we...
M E Cruzen et al.
DNA sequence : the journal of DNA sequencing and mapping, 4(4), 243-248 (1994-01-01)
We have determined the nucleotide sequence of a cDNA coding human cysteinyl-tRNA synthetase. The predicted protein sequence of 638 amino acids has substantial sequence similarity to the E. coli cysteinyl-tRNA synthetase in the nucleotide-binding fold region that constitutes the potential...
J E Kim et al.
Nucleic acids research, 28(15), 2866-2872 (2000-07-25)
The amino acid sequence of human cytoplasmic cysteinyl-tRNA synthetase (CRS) was examined by analyzing sequences of genomic and expressed sequence tag fragments. From theses analyses, a few interesting possibilities were suggested for the structure of human CRS. First, different isoforms...
Charlotte Stadler et al.
Journal of proteomics, 75(7), 2236-2251 (2012-03-01)
We have developed a platform for validation of antibody binding and protein subcellular localization data obtained from immunofluorescence using siRNA technology combined with automated confocal microscopy and image analysis. By combining the siRNA technology with automated sample preparation, automated imaging...

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