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2,3-Butanedione monoxime_Molecular_structure_CAS_57-71-6)
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2,3-Butanedione monoxime

Catalog No. B0753 Name Sigma Aldrich
CAS Number 57-71-6 Website http://www.sigmaaldrich.com
M. F. C4H7NO2 Telephone 1-800-521-8956
M. W. 101.10388 Fax
Purity ≥98% Email
Storage Chembase ID: 102404


IUPAC name
IUPAC Traditional name


PubChem SID 24277826
EC Number 200-348-5
Beilstein Number 605582
MDL Number MFCD00002116
CAS Number 57-71-6


Purity ≥98%
Gene Information human ... KCNB1(3745)
Boiling Point 185-186 °C(lit.)
Melting Point 75-78 °C(lit.)
Personal Protective Equipment Eyeshields, Gloves, type N95 (US), type P1 (EN143) respirator filter
RTECS EK3150000
German water hazard class 3


Description (简体中文)
1 kg in poly bottle
25, 100, 500 g in poly bottle
Biochem/physiol Actions
DRK1 is a delayed rectifier (Kv2.1) cloned K+ channel from rat brain with consensus sites for protein kinase-dependent phosphorylation that might be expected to be functionally regulated by phosphorylation. 2,3-Butanedione monoxime (BDM) chemically removes phosphate groups from many proteins, and its action on DRK1 channels was examined after expression of DRK1 cRNA in Xenopus oocytes. In two-microelectrode voltage-clamp experiments, the application of 2,3-Butanedione monoxime to the bath inhibited DRK1 current (ki = 16.6 mM, H = 0.96) rapidly and reversibly, with a time course similar to the time course of solution change within the bath. DRK1 current was inhibited at all potentials; the time course of current activation, deactivation and inactivation were unaffected by 2,3-Butanedione monoxime. In inside-out patch-clamp experiments, the application of 2,3-Butanedione monoxime to the cytoplasmic surface similarly inhibited channel activity rapidly and reversibly (ki = 10.7 mM, H = 1.01) in the absence of rephosphorylating substrates. These results are inconsistent with a phosphatase effect, because such an effect should be irreversible in cell-free, ATP-free patches. Instead, the results suggest that 2,3-Butanedione monoxime can inhibit DRK1 channels directly from inside or outside of the membrane.