CA200634 CellAura fluorescent adenosine antagonist [XAC]

Technical documents: SDS CoA Datasheet

Product overview

Name CA200634 CellAura fluorescent adenosine antagonist [XAC]
Biological description Competitive fluorescent adenosine receptor antagonist (apparent KD values are 7.50, 7.37 and 7.30 for A2A, A3 and A1 respectively). Antagonizes the activity of NECA, an adenosine receptor agonist. Inhibits cAMP accumulation and stimulates inositol phosphate accumulation (pKb values are 6.4 and 6.5 respectively). Exhibits no intrinsic agonist activity.
Alternative names Fluorescent Adenosine receptor Antagonist (A-633-AN), A-633-AN, XAC-X-BY630
Purity >97%
Description Competitive fluorescent adenosine receptor antagonist
Write Your Own Review
You're reviewing:CA200634 CellAura fluorescent adenosine antagonist [XAC]
Rate this item:


Figure 1. A2A-SPAP cells assayed against NECA and 1 µM HB7814
Figure 2. A3-SPAP cells assayed against NECA and 1 µM HB7814

Fluorescence imaging with HB7814

HB7814(30 nM) binding to live CHO cells expressing adenosine A1 receptors. Binding blocked by unlabelled competitor XAC (10 µM). Nuclei counter-stained with Hoechst.
CA200634 CellAura fluorescent adenosine antagonist [XAC]: Scientist Approved

Biological Data

Application notes For ligand binding; fluorescence imaging; high content analysis; kinetic analysis; cell sorting at adenosine A1 / A2A / A3 receptors use solutions up to 100 nM.
Pharmacological validation The CellAura fluorescent adenosine antagonist [XAC] ligand was shown to antagonize the activity of the adenosine receptor agonist adenosine-5'-N-ethyluronamide (NECA), in three separate recombinant CHO cell lines expressing the human A1, A2A or A3 receptor and a cyclic AMP-responsive secreted placental alkaline phosphatase (SPAP) reporter gene.The cyclic AMP-induced expression of SPAP was measured under basal and forskolin-stimulated (maximal) conditions. Addition of CellAura fluorescent adenosine antagonist [XAC] to the basal or forskolin-stimulated cells did not significantly alter basal and stimulated SPAP levels, demonstrating that CellAura fluorescent adenosine antagonist [XAC] has no intrinsic agonist activity.To determine the apparent KD for CellAura fluorescent adenosine antagonist [XAC], cells were treated with varying concentrations of NECA alone, or in the presence of 1µM CellAura fluorescent adenosine antagonist [XAC], and the cyclic AMP-induced expression of SPAP measured.The apparent KD at A1, A2A and A3 receptors was calculated from the rightward shift of the agonist response curve in the presence of CellAura fluorescent adenosine antagonist [XAC], compared to the response curve for the agonist alone, for each receptor-expressing cell line.

Solubility & Handling

Storage instructions -20°C (protect from light)
Solubility overview Soluble in DMSO
Handling After thawing individual aliquots for use, we recommend briefly sonicating the sample to ensure it is fully dissolved and the solution is homogeneous. We do not recommend using the product after subjecting it to repetitive freeze-thaw cycles.
Shipping conditions The product, supplied in a dry form, is stable at ambient temperature for periods of up to a few days and does not require shipping on ice/dry ice.
Important This product is for RESEARCH USE ONLY and is not intended for therapeutic or diagnostic use. Not for human or veterinary use.



More Info


More Info

Chemical Data

Purity >97%
Molecular Weight 974
Source Synthetic
Appearance Purple solid
Formulation Lyophilized film
Excitation 636 nm
Emission 651 nm
These publications cite the use of CA200634 CellAura fluorescent adenosine antagonist [XAC] purchased from Hello Bio:
  • The ADORA1 mutation linked to early-onset Parkinson's disease alters adenosine A(1)-A(2A) receptor heteromer formation and function.

    Sarasola LI et al (2022) Biomedicine & pharmacotherapy 156 : 113896
    PubMedID: 36279718
  • Functional solubilization of the β2-adrenoceptor using diisobutylene maleic acid

    Harwood CR et al (2021) iScience 24(12) : 103362
    PubMedID: 34825145
  • Allosteric Antagonism of the A2A Adenosine Receptor by a Series of Bitopic Ligands

    Gao ZG et al (2020) Cells 9(5)
    PubMedID: 32408534
  • Conversion of a non-selective adenosine receptor antagonist into A3-selective high affinity fluorescent probes using peptide-based linkers.

    Vernall AJ et al. (2013) Org Biomol Chem 11(34) : 5673-82.
    PubMedID: 23881285
  • Fluorescent ligands for adenosine receptors.

    Kozma E et al. (2013) Bioorg Med Chem Lett 23(1) : 26-36.
    PubMedID: 23200243

Items 1 to 5 of 12 total