N9879
NADase from porcine brain
≥0.007 unit/mg solid
Synonym(s):
DPN Nucleosidase, NAD+ glycohydrolase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
form
powder
Quality Level
specific activity
≥0.007 unit/mg solid
solubility
insoluble
storage temp.
−20°C
General description
NADase is a glycohydrolase that catalyzes ADP-ribose transfer.
Application
NADase from porcine brain has been used in a study to investigate histidine and related compounds resulting from catalyzed ADP-riboslyation. It has also been used in a study to investigate the preparation of arylazide-substituted pyridine adenine dinucleotides for photoaffinity labeling.
Biochem/physiol Actions
Nicotinamide has been shown to inhibit NADase activity.
Unit Definition
One unit will hydrolyze 1.0 μmole of β-NAD to nicotinamide and ADP-ribose per min at pH 7.3 at 37 °C.
Physical form
Acetone-dried powder
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Evidence for Enzymatic ADP-Ribosylation to Histidine and Related Dipeptides
Tono-oka, S., et al.
Acta Chemica Scandinavica, 48, 780-782 (1994)
Andrew D Napper et al.
Journal of medicinal chemistry, 48(25), 8045-8054 (2005-12-13)
High-throughput screening against the human sirtuin SIRT1 led to the discovery of a series of indoles as potent inhibitors that are selective for SIRT1 over other deacetylases and NAD-processing enzymes. The most potent compounds described herein inhibit SIRT1 with IC50
Drug-resistant virus has reduced ability to induce immune activation.
Rui Wang et al.
Journal of acquired immune deficiency syndromes (1999), 61(4), e60-e63 (2012-11-10)
Preparation and Evaluation of Arylazide-Substituted Pyridine Adenine Dinucleotides for Photoaffinity Labeling Experiments
Liu, W., et al.
Photochemistry and Photobiology, 63, 793-799 (1996)
Shoko Nakayama et al.
Hematology (Amsterdam, Netherlands), 17(6), 317-320 (2012-11-22)
The accurate determination of cytoplasmic immunoglobulin (cIg) light chain (LC) expression is important to differentiate reactive plasmacytosis from a clonal plasma cell neoplasm such as plasma cell myeloma (PCM). Through retrospective analysis, we studied the cytoplasmic kappa/lambda ratio of CD38-positive
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