NARS

  • Official Full Name

    asparaginyl-tRNA synthetase
  • Overview

    Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids.Asparaginyl-tRNA synthetase is localized to the cytoplasm and belongs to the class II family of tRNA synthetases.The N-terminal domain represents the signature sequence for the eukaryotic asparaginyl-tRNA synthetases.
  • Synonyms

    NARS;asparaginyl-tRNA synthetase;asparaginyl-tRNA synthetase, cytoplasmic;asparagine tRNA ligase 1;cytoplasmic;NARS1;3010001M15Rik;AA960128;ASNRS;ASNS;Asparagine tRNA ligase 1, cytoplasmic;Asparagine tRNA ligase;Asparagine--tRNA ligase;Asparaginyl tRNA synthetase;C78150;EC 6.1.1.22;LRRGT00113;MGC116236;NRS;SYNC_HUMAN

Recombinant Proteins

  • Mouse
  • Human
  • Chicken
  • Mycobacterium Tuberculosis
  • Mammalian Cell
  • Wheat Germ
  • E.coli
  • HEK293T
  • HEK293
  • Insect Cell
  • E.coli expression system
  • His
  • Non
  • His&T7
  • His&GST
  • Myc&DDK
  • His&Fc&Avi
Cat.# Product name Source (Host) Species Tag Protein Length Price
NARS-10431M Recombinant Mouse NARS Protein Mammalian Cell Mouse His
NARS-30281TH Recombinant Human NARS Wheat Germ Human Non 107 amino acids
NARS-3051C Recombinant Chicken NARS Mammalian Cell Chicken His
NARS-40H Recombinant Human NARS protein, His-tagged E.coli Human His
NARS-8205H Recombinant Human NARS protein, His & T7-tagged E.coli Human His&T7 Met1~Arg330
NARS-1167HCL Recombinant Human NARS cell lysate Human Non
Nars-1672M Recombinant Mouse Nars protein, His & GST-tagged E.coli Mouse His&GST Met1~Gly291
Nars-4294M Recombinant Mouse Nars Protein, Myc/DDK-tagged HEK293T Mouse Myc&DDK
NARS-4660H Recombinant Human NARS Protein (Met1-Arg330), His tagged E.coli Human His Met1-Arg330
NARS-5687H Recombinant Human NARS Protein, Myc/DDK-tagged, C13 and N15-labeled HEK293T Human Myc&DDK
NARS-5913M Recombinant Mouse NARS Protein, His (Fc)-Avi-tagged HEK293 Mouse His&Fc&Avi
NARS-5913M-B Recombinant Mouse NARS Protein Pre-coupled Magnetic Beads HEK293 Mouse
NARS-681H Recombinant Human NARS Protein (Met1-Pro548), His-tagged Insect Cell Human His Met1-Pro548
RFL11231MF Recombinant Full Length Probable Sensor Histidine Kinase Nars(Nars) Protein, His-Tagged E.coli expression system Mycobacterium Tuberculosis His Full L. Full Length (1-425)

    Involved Pathway

    NARS involved in several pathways and played different roles in them. We selected most pathways NARS participated on our site, such as Aminoacyl-tRNA biosynthesis, which may be useful for your reference. Also, other proteins which involved in the same pathway with NARS were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    Aminoacyl-tRNA biosynthesis FARSA,HARS2,TARS,VARS2,MADD,TARSL2,GATC,FARSB,CARS,WARS

    Protein Function

    NARS has several biochemical functions, for example, ATP binding,asparagine-tRNA ligase activity,nucleic acid binding. Some of the functions are cooperated with other proteins, some of the functions could acted by NARS itself. We selected most functions NARS had, and list some proteins which have the same functions with NARS. You can find most of the proteins on our site.

    Function Related Protein
    asparagine-tRNA ligase activity NARS2
    nucleic acid binding ZFP622,RBM4.1,ZFP14,KLF12A,INSM1B,UMPS,BICC2,REXO2,SFRS3A,EAR1
    ATP binding AFG3L2,AK5,TGFBR1B,JAK1,UPF1,TCP1,ATP2B2,MUSK,ACSS1,DNAJA3A

    Interacting Protein

    NARS 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 NARS here. Most of them are supplied by our site. Hope this information will be useful for your research of NARS.

    IKBKE;LSM1;ATXN1;deoB;ssrna_ug;FN1;IFI16;HDAC2

    Resources

    References

    • Kovalenko, OV; Olland, A; et al. Atypical Antigen Recognition Mode of a Shark Immunoglobulin New Antigen Receptor (IgNAR) Variable Domain Characterized by Humanization and Structural Analysis. JOURNAL OF BIOLOGICAL CHEMISTRY 288:17408-17419(2013).
    • Liu, NJ; Schnell, S; et al. Sex, Pain, and Opioids: Interdependent Influences of Sex and Pain Modality on Dynorphin-Mediated Antinociception in Rats. JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS 344:522-530(2013).

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