2418-69-1 Usage
Description
H-ARG-PRO-OH SULFATE SALT is a sulfated salt form of H-arginyl-L-proline, an amino acid dipeptide with potential antifibrotic and anti-angiogenic activities. It is used in various biochemical and pharmacological research applications.
Used in Pharmaceutical Industry:
H-ARG-PRO-OH SULFATE SALT is used as a therapeutic agent for its potential antifibrotic and anti-angiogenic properties. It is being studied for its potential therapeutic applications in diseases such as pulmonary fibrosis, liver fibrosis, and certain types of cancers.
Used in Biochemical Research:
H-ARG-PRO-OH SULFATE SALT is used as a research compound to study its potential inhibitory effects on prolyl 4-hydroxylase, an enzyme involved in collagen synthesis, and its ability to disrupt signaling pathways involved in angiogenesis.
Further research is needed to fully understand the mechanisms and potential benefits of H-ARG-PRO-OH SULFATE SALT in clinical settings.
Check Digit Verification of cas no
The CAS Registry Mumber 2418-69-1 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 2,4,1 and 8 respectively; the second part has 2 digits, 6 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 2418-69:
(6*2)+(5*4)+(4*1)+(3*8)+(2*6)+(1*9)=81
81 % 10 = 1
So 2418-69-1 is a valid CAS Registry Number.
InChI:InChI=1/C11H21N5O3/c12-7(3-1-5-15-11(13)14)9(17)16-6-2-4-8(16)10(18)19/h7-8H,1-6,12H2,(H,18,19)(H4,13,14,15)
2418-69-1Relevant articles and documents
Catalytic properties of X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris nTR.
Yan,Ho,Hou
, p. 704 - 707 (2007/10/02)
An X-prolyl dipeptidyl aminopeptidase (X-PDAP; EC 3.4.14.5) was identified to be loosely bound on the inner cell membrane fraction of Lactococcus lactis subsp. cremoris nTR. The biosynthesis of X-PDAP was continuously increased before the late-log growth phase of the bacteria. Both Gly-Pro-pNA and Ala-Ala-pNA were hydrolyzed by X-PDAP; the kcat/Km value of the former was about 10-fold that of the latter. The Ki of X-Pro and Pro-X were more specific to X-PDAP than those of X-Ala. The enzyme splitting a dipeptide sequentially from beta-casomorphin as a model catalytic pattern was identified and some properties of the enzyme were further characterized.