Recombinant human ADRB2 and GiaaS Asn280 fusion protein (ab90334)


  • Product name
    Recombinant human ADRB2 and GiaaS Asn280 fusion protein
  • Protein length
    Full length protein


  • Nature
  • Source
    Baculovirus infected Sf9 cells
  • Amino Acid Sequence
    • Species
    • Molecular weight
      98 kDa
    • Additional sequence information
      Tagged at the N terminus of the ADRB2 with a DDDDK tag. The C terminus of the ADRB2 is linked to the N terminus of the GiaaS Asn280 with a His tag.


Our Abpromise guarantee covers the use of ab90334 in the following tested applications.

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

  • Biological activity
    ab90334 exhibits high-affinity XTPase activity.
    Activity: 1.2 - 3 pmol/mg.
  • Applications

    Functional Studies

  • Form
  • Additional notes

    The beta 2 Adrenergic Receptor-GsalphaS-Asn280 fusion protein ensures a defined 1:1 stoichiometry of the receptor and the GsalphaS-Asn280 subunit as well as high coupling efficiency.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents: 75mM Tris HCl, 12.5mM Magnesium chloride, 1mM EDTA, pH 7.4

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

General Info

  • Relevance
    ADRB2 is activated by the catecholamine epinephrine and couples to the G-protein Gs to mediate adeylate cyclase activation. ADRB2 is found in numerous tissues and cell types including vascular and bronchial smooth muscle cells, leukocytes and liver. ADRB2 mediates smooth muscle relaxation, inhibition of leukocyte function and activation of glycogenolysis. GaaS is the short splice variant of the alpha; subunit of the heterotrimeric G-protein Gs. Gs activates the effector adenylate cyclase. GaaS differs from the long splice variant (GsaL) by the absence of a 15-amino acid insert between the ras-like domain and the a-helical domain. GaaS possesses a higher GDP-affinity than GaaL. GTP-binding proteins possess a highly conserved aspartate residue in the NKXD motif that is critical for high-affinity interaction with GTP. In small GTP-binding proteins, the D/N-mutation switches base-specifity from guanine to xanthine. In contrast to all other known Ga D/N mutants, the exchange of Asp280 to Asn280 in GaaS does not lead to an inactivation in nucleotide binding. The D/N mutant is a Gaa with specificity for XTP and XppNHp relative to GTP and GppNHp respectively. However, the mutant is not specific for XTPgS relative to GTPgS probably because of conformational alterations in the catalytic site by the g-thiophosphate.

References for Recombinant human ADRB2 and GiaaS Asn280 fusion protein (ab90334)

ab90334 has not yet been referenced specifically in any publications.

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