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Boc-Lys(Boc)-ONp, also known as Nα,Nε-DiBoc-L-lysine p-Nitrophenol Ester, is a light yellowish crystalline powder that serves as an antibody-drug conjugate and antitumor agent. Its chemical properties make it a valuable compound in the field of pharmaceuticals and medicine.

2592-19-0

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2592-19-0 Usage

Uses

Used in Pharmaceutical Industry:
Boc-Lys(Boc)-ONp is used as an antibody-drug conjugate for targeted cancer therapy. It is designed to deliver antitumor agents directly to cancer cells, minimizing damage to healthy cells and reducing side effects.
Used in Antitumor Applications:
Boc-Lys(Boc)-ONp is used as an antitumor agent for the treatment of various types of cancer. Its targeted approach allows for more effective and precise delivery of therapeutic agents to cancer cells, improving treatment outcomes and patient quality of life.

Check Digit Verification of cas no

The CAS Registry Mumber 2592-19-0 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 2,5,9 and 2 respectively; the second part has 2 digits, 1 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 2592-19:
(6*2)+(5*5)+(4*9)+(3*2)+(2*1)+(1*9)=90
90 % 10 = 0
So 2592-19-0 is a valid CAS Registry Number.
InChI:InChI=1/C22H33N3O8/c1-21(2,3)32-19(27)23-14-8-7-9-17(24-20(28)33-22(4,5)6)18(26)31-16-12-10-15(11-13-16)25(29)30/h10-13,17H,7-9,14H2,1-6H3,(H,23,27)(H,24,28)

2592-19-0 Well-known Company Product Price

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  • Alfa Aesar

  • (H62949)  Nalpha,Nepsilon-Di-Boc-L-lysine 4-nitrophenyl ester, 98%   

  • 2592-19-0

  • 5g

  • 353.0CNY

  • Detail
  • Alfa Aesar

  • (H62949)  Nalpha,Nepsilon-Di-Boc-L-lysine 4-nitrophenyl ester, 98%   

  • 2592-19-0

  • 25g

  • 1411.0CNY

  • Detail

2592-19-0SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 15, 2017

Revision Date: Aug 15, 2017

1.Identification

1.1 GHS Product identifier

Product name BOC-LYS(BOC)-ONP

1.2 Other means of identification

Product number -
Other names N,N'-DiBoc-L-lysine p-nitrophenol ester

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:2592-19-0 SDS

2592-19-0Relevant academic research and scientific papers

Identification and characterization of a periplasmic aminoacyl- phosphatidylglycerol hydrolase responsible for Pseudomonas aeruginosa lipid homeostasis

Arendt, Wiebke,Groenewold, Maike K.,Hebecker, Stefanie,Dickschat, Jeroen S.,Moser, Juergen

, p. 24717 - 24730 (2013/09/23)

Background: Continuous adaptation of the bacterial membrane is required in response to changing environmental conditions. Results: Pseudomonas aeruginosa ORF PA0919 codes for an alanyl-phosphatidylglycerol hydrolase that is anchored to the periplasmic surface of the inner membrane. Conclusion: The elucidated enzymatic activity implies a new regulatory circuit for the fine tuning of cellular alanyl-phosphatidylglycerol concentrations. Significance: Lipid homeostasis is crucial for understanding antimicrobial susceptibility. Specific aminoacylation of the phospholipid phosphatidylglycerol (PG) with alanine (or with lysine) was shown to render various organisms less susceptible to antimicrobial agents and environmental stresses. In this study, we make use of the opportunistic pathogen Pseudomonas aeruginosa to decode ORF PA0919-dependent lipid homeostasis. Analysis of the polar lipid content of the deletion mutant ΔPA0919 indicated significantly enlarged levels of alanyl-PG. The resulting phenotype manifested an increased susceptibility to several antimicrobial compounds when compared with the wild type. A pH-dependent PA0919 promoter located within the upstream gene PA0920 was identified. Localization experiments demonstrated that the PA0919 protein is anchored to the periplasmic surface of the inner bacterial membrane. The recombinant overproduction of wild type and several site-directed mutant proteins in the periplasm of Escherichia coli facilitated a detailed in vitro analysis of the enzymatic PA0919 function. A series of artificial substrates (p-nitrophenyl esters of various amino acids/aliphatic acids) indicated enzymatic hydrolysis of the alanine, glycine, or lysine moiety of the respective ester substrates. Our final in vitro activity assay in the presence of radioactively labeled alanyl-PG then revealed hydrolysis of the aminoacyl linkage, resulting in the formation of alanine and PG. Consequently, PA0919 was termed alanyl-PG hydrolase. The elucidated enzymatic activity implies a new regulatory circuit for the appropriate tuning of cellular alanyl-PG concentrations.

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