dars
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  • Official Full Name
  • aspartyl-tRNA synthetase
  • Background
  • Aspartyl-tRNA synthetase (DARS) is part of a multienzyme complex of aminoacyl-tRNA synthetases.Aspartyl-tRNA synthetase charges its cognate tRNA with aspartate during protein biosynthesis.
  • Synonyms
  • DARS; aspartyl-tRNA synthetase; aspartate--tRNA ligase, cytoplasmic; aspartate tRNA ligase 1; cytoplasmic; aspRS; aspartate tRNA ligase 1, cytoplasmic; aspartyl-tRNA synthetase, cytoplasmic; cell proliferation-inducing protein 40; cell proliferation-induc
Cat.#:DARS-2348HTag:GST
Source (Host):Wheat GermSpecies:Human
Product nameRecombinant Human DARS Protein, GST-tagged
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Cat.#:DARS-11831HTag:GST
Source (Host):E. coliSpecies:Human
Product nameRecombinant Human DARS, GST-tagged
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Cat.#:DARS-3672HTag:His
Source (Host):Mammalian CellsSpecies:Human
Product nameRecombinant Human DARS, His-tagged
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Cat.#:DARS-564HTag:His
Source (Host):E. coliSpecies:Human
Product nameRecombinant Human DARS, His tagged
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Cat.#:DARS-8220HTag:His/T7
Source (Host):E. coliSpecies:Human
Product nameRecombinant Human DARS protein, His & T7-tagged
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Cat.#:Dars-3671RTag:His
Source (Host):Mammalian CellsSpecies:Rat
Product nameRecombinant Rat Dars, His-tagged
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Cat.#:DARS-1666CTag:His
Source (Host):Mammalian CellsSpecies:Chicken
Product nameRecombinant Chicken DARS
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Cat.#:DARS-4805ZTag:His
Source (Host):Mammalian CellsSpecies:Zebrafish
Product nameRecombinant Zebrafish DARS
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Cat.#:DARS-7073HCLTag:
Source (Host):Species:Human
Product nameRecombinant Human DARS 293 Cell Lysate
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Involved Pathway

DARS involved in several pathways and played different roles in them. We selected most pathways DARS participated on our site, such as Alanine and aspartate metabolism, Aminoacyl-tRNA biosynthesis, Cytosolic tRNA aminoacylation, which may be useful for your reference. Also, other proteins which involved in the same pathway with DARS were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name
Pathway Related Protein
Alanine and aspartate metabolism
DARS; AGXT; ABAT
Aminoacyl-tRNA biosynthesis
HARS2; RARS2; MADD; RARS; DARS; IARS; LARS2; AARS2; MARS2; QRSL1
Cytosolic tRNA aminoacylation
KARS; AARS; FARSB; AIMP1; EEF1E1; DARS; AIMP2; MADD
Gene Expression
ZNF554; NR5A1B; GATAD2B; ZNF75D; MADD; BARHL1; MTF2; RNF111; PTRFB; ZNF18
tRNA Aminoacylation
KARS; AIMP1; AARS; FARS2; DARS; WARS2; AIMP2; MADD; EEF1E1; FARSB

Protein Function

DARS has several biochemical functions, for example, ATP binding, aminoacylase activity, aspartate-tRNA ligase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by DARS itself. We selected most functions DARS had, and list some proteins which have the same functions with DARS. You can find most of the proteins on our site.
Function
Related Protein
Function ATP binding
Related Protein AURKA; MYO1H; KIF2B; MAPK12B; Aatk; SPHK2; KIF9; MOS; ABCA1B; ATP2C1
Function aminoacylase activity
Related Protein CAT; ASPA; ACY3; ACY1; DARS
Function aspartate-tRNA ligase activity
Related Protein DARS; DARS2
Function poly(A) RNA binding
Related Protein SRP72; PDCD11; PWP2; RRP36; TMEM38A; EMG1; SMG1; ZFC3H1; QK; CCDC108
Function protein binding
Related Protein FAM92A; KCNG4; PPIG; CORO1A; C7orf25; PLSCR4; CHN1; SLC14A2; LINGO1; ATP6V1F

Interacting Protein

DARS has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with DARS here. Most of them are supplied by our site. Hope this information will be useful for your research of DARS.
AIMP2; GRB2; gag; MAP3K7; PIK3R1; NDRG1; TNFRSF10D; HSP90AA1; yndJ; PIK3R3; 15-deoxy-delta(12,14

DARS Related Articles

Kozak, KR; Tsai, SP; et al. Total Antibody Quantification for MMAE-Conjugated Antibody-Drug Conjugates: Impact of Assay Format and Reagents. BIOCONJUGATE CHEMISTRY 24:772-779(2013).
Brenke, R; Hall, DR; et al. Application of asymmetric statistical potentials to antibody-protein docking. BIOINFORMATICS 28:2608-2614(2012).