1093-96-5 Usage
Uses
Used in Biochemical and Clinical Chemistry Research:
Dansylsarcosine is used as a substrate for measuring the activity of transporter proteins, particularly those involved in the transport of organic anions across cell membranes. It aids in the study of the function and regulation of these proteins, which is crucial for understanding various biological processes and disease mechanisms.
Used as a Standard Compound in Chromatographic Analysis:
Dansylsarcosine serves as a reference material in analytical chemistry, specifically in chromatographic techniques. Its fluorescent properties make it an ideal standard for calibration and quality control in these analyses, ensuring accurate and reliable results.
Used as a Potential Biomarker for Disease and Condition Studies:
Due to its interaction with transporter proteins, dansylsarcosine has been investigated for its potential as a biomarker for various diseases and conditions related to transporter dysfunction. This application could lead to improved diagnostics and therapeutic strategies for such conditions.
Check Digit Verification of cas no
The CAS Registry Mumber 1093-96-5 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 1,0,9 and 3 respectively; the second part has 2 digits, 9 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 1093-96:
(6*1)+(5*0)+(4*9)+(3*3)+(2*9)+(1*6)=75
75 % 10 = 5
So 1093-96-5 is a valid CAS Registry Number.
InChI:InChI=1/C15H18N2O4S/c1-16(2)13-8-4-7-12-11(13)6-5-9-14(12)22(20,21)17(3)10-15(18)19/h4-9H,10H2,1-3H3,(H,18,19)
1093-96-5Relevant academic research and scientific papers
A fluorescent probe for butyrylcholinesterase activity in human serum based on a fluorophore with specific binding affinity for human serum albumin
Han, Min Su,Yoo, Soyeon
supporting information, p. 14574 - 14577 (2019/12/11)
Non-specific binding of a fluorescent probe to human serum albumin is problematic because it induces signal interference when the probe detects the target biomarker in human serum. To eliminate this problem, we used intrinsically problematic non-specific fluorescence in designing a fluorescent probe for butyrylcholinesterase activity in serum. The probe containing a fluorophore with specific binding affinity for albumin could sensitively detect butyrylcholinesterase activity in serum with high selectivity to acetylcholinesterase and screen the efficiency of butyrylcholinesterase inhibitors.
