D0250
α-Dansyl-L-arginine hydrochloride
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经验公式（希尔记法）:
C18H25N5O4S · HCl
化学文摘社编号:
分子量:
443.95
NACRES:
NA.26
PubChem Substance ID:
UNSPSC Code:
12352200
EC Number:
248-904-6
MDL number:
InChI key
HRBPBWKDJGGGCX-UHFFFAOYSA-N
InChI
1S/C18H25N5O4S/c1-23(2)15-9-3-7-13-12(15)6-4-10-16(13)28(26,27)22-14(17(24)25)8-5-11-21-18(19)20/h3-4,6-7,9-10,14,22H,5,8,11H2,1-2H3,(H,24,25)(H4,19,20,21)
SMILES string
CN(C)c1cccc2c(cccc12)S(=O)(=O)NC(CCCNC(N)=N)C(O)=O
assay
≥98% (TLC)
form
powder
color
yellow to green
storage temp.
−20°C
Quality Level
Biochem/physiol Actions
α-Dansyl-L-arginine contains an N-terminal fluorophore (dansyl) making it useful as fluorescent marker/probe. α-Dansyl-L-arginine is used as a site specific marker for drug binding pockets on proteins. α-Dansyl-L-arginine, dansyl-l-asparagine, and dansyl-l-glutamate are specific for the site 1 drug binding site on albumin (HSA).
signalword
Danger
hcodes
pcodes
Hazard Classifications
Acute Tox. 3 Oral
存储类别
6.1D - Non-combustible acute toxic Cat.3 / toxic hazardous materials or hazardous materials causing chronic effects
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
P J McIlroy et al.
Endocrinology, 113(1), 222-227 (1983-07-01)
The effects of dansyl-arginyl-(4'-ethyl)-piperidine amide (DAPA) on the binding of gonadotropins has been investigated. The compound inhibited the binding of hCG, human LH, and porcine LH to rat luteal membranes with an ED50 of 70 microM and the binding of
J M Mesaros et al.
Analytical chemistry, 68(19), 3441-3449 (1996-10-01)
Continuous zone electrophoretic separations in narrow channels coupled to small-bore capillaries have been demonstrated and characterized previously. Presented here is the use of this new technique to monitor dynamic chemical changes occurring in a flow injection analysis system. The fundamental
N Muller et al.
The Journal of pharmacy and pharmacology, 46(4), 300-304 (1994-04-01)
Human serum albumin is known to have two major and selective drug binding sites, termed sites I and II. The fluorescent probes, dansylamide and dansylsarcosine selectively interact with sites I and II, respectively. However, the binding site of the fluorescent
Ali J Ryan et al.
Journal of structural biology, 174(1), 84-91 (2010-10-14)
Human serum albumin (HSA) has two primary binding sites for drug molecules. These sites selectively bind different dansylated amino acid compounds, which-due to their intrinsic fluorescence-have long been used as specific markers for the drug pockets on HSA. We present
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