144000-36-2 Usage
Description
(H-D-CYS-OME)2 2 HCL, also known as D-Cystine Dimethyl Ester Dihydrochloride, is an amino acid derivative characterized by its white to off-white powder form. It is primarily used as a reagent in various applications due to its unique chemical properties.
Uses
Used in Pharmaceutical Industry:
(H-D-CYS-OME)2 2 HCL is used as a reagent for the synthesis of various pharmaceutical compounds. Its application is based on its amino acid derivative nature, which allows for the creation of new drug molecules with potential therapeutic benefits.
Used in Research and Development:
In the field of research and development, (H-D-CYS-OME)2 2 HCL serves as a crucial reagent for conducting experiments and developing new methodologies. Its role is to facilitate the exploration of novel chemical reactions and the synthesis of innovative compounds with potential applications in various industries.
Used in Biochemical Applications:
(H-D-CYS-OME)2 2 HCL is utilized as a reagent in biochemical applications, where it aids in the study of protein structure and function. Its amino acid derivative nature makes it a valuable tool for understanding the interactions between proteins and other biomolecules, contributing to the advancement of biochemistry and molecular biology.
Used in Cosmetics Industry:
In the cosmetics industry, (H-D-CYS-OME)2 2 HCL is used as a reagent for the development of skincare products. Its application is based on its ability to enhance the formulation of creams, lotions, and other skincare products, potentially improving their efficacy and performance.
Used in Agricultural Industry:
(H-D-CYS-OME)2 2 HCL is employed as a reagent in the agricultural industry, where it is used for the development of new pesticides, fertilizers, and other agrochemicals. Its role is to contribute to the creation of more effective and environmentally friendly products for crop protection and enhancement.
Check Digit Verification of cas no
The CAS Registry Mumber 144000-36-2 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,4,4,0,0 and 0 respectively; the second part has 2 digits, 3 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 144000-36:
(8*1)+(7*4)+(6*4)+(5*0)+(4*0)+(3*0)+(2*3)+(1*6)=72
72 % 10 = 2
So 144000-36-2 is a valid CAS Registry Number.
144000-36-2Relevant articles and documents
CYSTINE DIAMIDE ANALOGS FOR CYSTINURIA
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Paragraph 0024; 0171-0172, (2021/06/22)
This document discloses novel cystine analogs, methods of making cystine analogs, compositions containing cystine analogs and methods of using such analogs for inhibiting cystine stone formation and treatment of cystinuria.
Defining the dimensions of the catalytic site of phospholipase A2 using amide substrate analogues
Yu, Lin,Dennis, Edward A.
, p. 8757 - 8762 (2007/10/02)
Two series of phospholipid analogues, each containing a thioether function at the sn-1 position and an amide function at the sn-2 position, have been synthesized and evaluated as phospholipase A2 inhibitors. The first series of analogues contained a hexyl group (C-6) at the sn-1 position and various acyl groups at the sn-2 position, ranging from formyl to dodecanoyl (1-12 carbons). The second series contained an sn-1 hexadecyl group (C-16) and various sn-2 acyl groups from formyl to eicosanoyl (1-20 carbons). Hydrophobic interactions of the enzyme with the amide analogues were studied using several different substrate forms including monomers, micelles, and mixed micelles with Triton X-100. The C-6 amide analogues were used for the monomeric study while the C-16 analogues were used in the micellar studies. The inhibition studies with the monomeric amide analogues demonstrate that the sn-2 acyl chain is absolutely required for the binding of the analogue to the enzyme and that the catalytic site interacts with about the first 10 carbons of the sn-2 acyl chain. In addition, each methylene group of the sn-2 acyl chain from C5 to C10 provides about 665 cal/mol of binding energy. In contrast, the inhibition potency of the amide analogues in micellar states followed a quite different, more complex chain length dependency. The chain length of the sn-21 acyl group is much less important in the micellar systems than in the monomeric system, since the hydrophobic interactions between the sn-2 acyl chain and the enzyme are balanced by its interactions with the hydrophobic core of the micelle. The importance of double bonds in the sn-2 chain was also studied, but no correlation between the degree of unsaturation and the degree of inhibition was observed. These studies help delineate the mode of the interactions between enzyme and substrate.
