Description

  • Product name

    Recombinant human AlaRS protein
  • Biological activity

    ab73442 is reactive against Polymyositis sera.
  • Purity

    > 90 % SDS-PAGE.
    ab73442 is purified by proprietary chromatographic techniques.
  • Expression system

    Baculovirus infected Sf9 cells
  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Predicted molecular weight

      108 kDa
    • Additional sequence information

      Alanyl-tRNA synthetase Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 107,598 Dalton

Specifications

Our Abpromise guarantee covers the use of ab73442 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Western blot

    ELISA

    SDS-PAGE

  • Form

    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.3808% HEPES, 20% Glycerol, 1.45% Sodium chloride

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names

    • AARS
    • AI316495
    • Alanine tRNA ligase
    • Alanine tRNA ligase 1, cytoplasmic
    • Alanine tRNA ligase cytoplasmic
    • Alanine--tRNA ligase
    • Alanyl tRNA synthetase
    • Alanyl tRNA synthetase cytoplasmic
    • Alanyl-tRNA synthetase
    • AlaRS
    • C76919
    • CMT2N
    • cytoplasmic
    • EC 6.1.1.7
    • MGC37368
    • Renal carcinoma antigen NY REN 42
    • Renal carcinoma antigen NY-REN-42
    • SYAC_HUMAN
    see all
  • Function

    Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
  • Involvement in disease

    Charcot-Marie-Tooth disease 2N
  • Sequence similarities

    Belongs to the class-II aminoacyl-tRNA synthetase family.
  • Domain

    Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
    The C-terminal C-Ala domain (residues 756 to 968), along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. The human domain can be used in vitro to replace the corresponding domain in E.coli.
  • Post-translational
    modifications

    ISGylated.
  • Cellular localization

    Cytoplasm.
  • Information by UniProt

References

ab73442 has not yet been referenced specifically in any publications.

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