ADP-HPD, Dihydrate, Ammonium Salt, ADP-HPD, Dihydrate is an amino analog of ADP-ribose that acts as a highly potent, noncompetitive, and specific inhibitor of poly(ADP-ribose) glycohydrolase (PARG; IC₅₀ = 120 nM).
OK to freeze desiccated (hygroscopic) protect from light
color
white
solubility
water: 5 mg/mL
shipped in
ambient
storage temp.
−20°C
General description
An amino analog of ADP-ribose that acts as a highly potent, noncompetitive, and specific inhibitor of poly(ADP-ribose) glycohydrolase (PARG) (IC50 = 120 nM) vs. ADP-ribose (IC50 = 120 mM). Also inhibits NAD glycohydrolase from Bungarus fasciatus venom at much higher concentrations (IC50 = 260 µM). Does not affect the activities of either poly(ADP-ribose) polymerase (PARP) or NAD:arginine mono(ADP-ribosyl)-transferase A even at 1 mM concentration.
An amino analog of ADP-ribose that acts as a highly potent, noncompetitive, and specific inhibitor of poly(ADP-ribose) glycohydrolase (PARG; IC50 = 120 nM). Does not affect the activities of either poly(ADP-ribose) polymerase (PARP) or NAD:arginine mono(ADP-ribosyl)-transferase A even at 1 mM concentration. Also acts as an inhibitor of NAD glycohydrolase from Bungarus fasciatus venom at much higher concentrations (IC50 = 260 µM). Note: 1 set = 5 x 60 µg.
Note: 1 set = 5 x 60 µg
Biochem/physiol Actions
Cell permeable: no
Primary Target PARG
Product does not compete with ATP.
Reversible: no
Target IC50: 120 nM against poly(ADP-ribose) glycohydrolase (PARG)
Packaging
Packaged under inert gas
Warning
Toxicity: Standard Handling (A)
Reconstitution
Following reconstitution, aliquot and freeze at -20°C. Stock solutions are stable for up to 1 week at -20°C.
Other Notes
Vispe, S., et al. 2000. Proc. Natl. Acad. Sci. USA97, 9886. Slama, J.T., et al. 1995. J. Med. Chem.38, 389. Slama, J.T., et al. 1995. J. Med. Chem.38, 4332.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Mass spectrometry-enabled ADP-ribosylation workflows are developing rapidly, providing researchers a variety of ADP-ribosylome enrichment strategies and mass spectrometric acquisition options. Despite the growth spurt in upstream technologies, systematic ADP-ribosyl (ADPr) peptide mass spectral annotation methods are lacking. HCD-dependent ADP-ribosylome studies
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