A3261
Arg-Arg β-萘酰胺 三盐酸盐
≥99% (HPLC), powder
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关于此项目
经验公式（希尔记法）:
C22H33N9O2 · 3HCl
化学文摘社编号:
分子量:
564.94
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32
MDL number:
产品名称
Arg-Arg β-萘酰胺 三盐酸盐,
SMILES string
Cl.Cl.Cl.N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)Nc1ccc2ccccc2c1
InChI
1S/C22H33N9O2.3ClH/c23-17(7-3-11-28-21(24)25)19(32)31-18(8-4-12-29-22(26)27)20(33)30-16-10-9-14-5-1-2-6-15(14)13-16;;;/h1-2,5-6,9-10,13,17-18H,3-4,7-8,11-12,23H2,(H,30,33)(H,31,32)(H4,24,25,28)(H4,26,27,29);3*1H/t17-,18-;;;/m0.../s1
InChI key
RNVXXFQJTJQVER-NCXIRTITSA-N
assay
≥99% (HPLC)
form
powder
solubility
water: 50 mg/mL, clear, colorless to faintly yellow
storage temp.
−20°C
Quality Level
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Application
Arg-Arg β-naphthylamide trihydrochloride has been used as a substrate for the enzyme dipeptidyl peptidase 3 expressed in human embryonic kidney cells (HEK293T) and as a substrate for peptidase from black-pigmented bacteroides (BPB) and spirochetes.
General description
Arg-Arg β-naphthylamide is a dipeptide and a β-naphthylamide derivative.
Substrate for dipeptidyl aminopeptidase III.
Mammalian lens dipeptidyl aminopeptidase III.
A A Swanson et al.
Biochemical and biophysical research communications, 84(4), 1151-1159 (1978-10-30)
Identification of periodontopathic bacteria based upon their peptidase activities.
H Suido et al.
Advances in dental research, 2(2), 304-309 (1988-11-01)
S A Chan et al.
Biochemical and biophysical research communications, 127(3), 962-968 (1985-03-29)
Extracts prepared from culminating cells of Dictyostelium discoideum have been found to contain dipeptidyl-aminopeptidases I (EC 3.4.14.1), II (EC 3.4.14.2), III (EC 3.4.14.4), arginine aminopeptidase (EC 3.4.11.6) and valine aminopeptidase. Dipeptidyl-aminopeptidase III was the most active of the dipeptidyl-aminopeptidases; its
Dipeptidyl arylamidase III of the pituitary. Purification and characterization.
S Ellis et al.
The Journal of biological chemistry, 242(20), 4623-4629 (1967-10-25)
Heung Sik Hahm et al.
Nature chemical biology, 16(2), 150-159 (2019-11-27)
Covalent probes serve as valuable tools for global investigation of protein function and ligand binding capacity. Despite efforts to expand coverage of residues available for chemical proteomics (e.g., cysteine and lysine), a large fraction of the proteome remains inaccessible with
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