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16709-12-9

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16709-12-9 Usage

General Description

H-ALA-ARG-OH is a chemical compound consisting of three amino acids: alanine (ALA), arginine (ARG), and a carboxylic acid group (OH). These amino acids are essential building blocks of proteins and play a crucial role in various biological processes within the body. Alanine is a non-essential amino acid that helps regulate blood sugar levels and strengthens the immune system, while arginine is a semi-essential amino acid that is involved in the production of nitric oxide, which supports cardiovascular health and blood flow. The carboxylic acid group serves as a functional group in the compound, allowing it to participate in chemical reactions and contribute to its overall structure and properties. The combination of these three components in H-ALA-ARG-OH makes it a valuable compound in the study of biochemistry and pharmaceuticals.

Check Digit Verification of cas no

The CAS Registry Mumber 16709-12-9 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,6,7,0 and 9 respectively; the second part has 2 digits, 1 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 16709-12:
(7*1)+(6*6)+(5*7)+(4*0)+(3*9)+(2*1)+(1*2)=109
109 % 10 = 9
So 16709-12-9 is a valid CAS Registry Number.

16709-12-9SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 16, 2017

Revision Date: Aug 16, 2017

1.Identification

1.1 GHS Product identifier

Product name (2S)-2-[[(2S)-2-aminopropanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid

1.2 Other means of identification

Product number -
Other names -

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:16709-12-9 SDS

16709-12-9Relevant articles and documents

Identification and characterization of prokaryotic dipeptidyl-peptidase 5 from porphyromonas gingivalis

Ohara-Nemoto, Yuko,Rouf, Shakh M. A.,Naito, Mariko,Yanase, Amie,Tetsuo, Fumi,Ono, Toshio,Kobayakawa, Takeshi,Shimoyama, Yu,Kimura, Shigenobu,Nakayama, Koji,Saiki, Keitarou,Konishi, Kiyoshi,Nemoto, Takayuki K.

, p. 5436 - 5448 (2014/03/21)

Porphyromonas gingivalis, a Gram-negative asaccharolytic anaerobe, is a major causative organism of chronic periodontitis. Because the bacterium utilizes amino acids as energy and carbon sources and incorporates them mainly as dipeptides, a wide variety of dipeptide production processes mediated by dipeptidyl-peptidases (DPPs) should be beneficial for the organism. In the present study, we identified the fourth P. gingivalis enzyme, DPP5. In a dpp4-7-11-disrupted P. gingivalis ATCC 33277, a DPP7-like activity still remained. PGN-0756 possessed an activity indistinguishable from that of the mutant, and was identified as a bacterial orthologue of fungal DPP5, because of its substrate specificity and 28.5% amino acid sequence identity with an Aspergillus fumigatus entity. P. gingivalis DPP5 was composed of 684 amino acids with a molecular mass of 77,453, and existed as a dimer while migrating at 66 kDa on SDS-PAGE. It preferred Ala and hydrophobic residues, had no activity toward Pro at the P1 position, and no preference for hydrophobic P2 residues, showed an optimal pH of 6.7 in the presence of NaCl, demonstrated Km and kcat/Km values for Lys-Ala-MCA of 688 μM and 11.02 μM-1 s-1, respectively, and was localized in the periplasm. DPP5 elaborately complemented DPP7 in liberation of dipeptides with hydrophobic P1 residues. Examinations of DPP- and gingipain gene-disrupted mutants indicated that DPP4, DPP5, DPP7, and DPP11 together with Arg- and Lys-gingipains cooperatively liberate most dipeptides from nutrient oligopeptides. This is the first study to report that DPP5 is expressed not only in eukaryotes, but also widely distributed in bacteria and archaea.

A NEW FLUOROGENIC SUBSTRATE OF CARBOXYPEPTIDASE H - o-COUMAROYLPHENYLALANYLALANYLARGININE

Pozdnev, V. F.,Varlamov, O. L.,Grigor'yants, O. O.,Gomazkov, O. A.

, p. 213 - 218 (2007/10/02)

A new fluorogenic substrate is proposed for determining the enzymatic activity of carboxypeptidase H - o-coumaryl-L-phenylalanyl-L-alanyl-L-arginine (Cum-Phe-Ala-Arg-OH).The enzymatic hydrolysis of the substrate forms Cum-Phe-Ala-OH, which is determined f

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