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89187-15-5

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89187-15-5 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 89187-15-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 8,9,1,8 and 7 respectively; the second part has 2 digits, 1 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 89187-15:
(7*8)+(6*9)+(5*1)+(4*8)+(3*7)+(2*1)+(1*5)=175
175 % 10 = 5
So 89187-15-5 is a valid CAS Registry Number.

89187-15-5SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 19, 2017

Revision Date: Aug 19, 2017

1.Identification

1.1 GHS Product identifier

Product name L-Isoleucine, glycyl-L-prolyl-

1.2 Other means of identification

Product number -
Other names L-Isoleucine, N-(1-glycyl-L-prolyl)-

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:89187-15-5 SDS

89187-15-5Downstream Products

89187-15-5Relevant 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.

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