61464-33-3

Basic information

• Product Name: Z-ASP(OBZL)-OSU
• Synonyms: Z-ASPARTIC ACID(OBZL)-OSU;Z-ASP(OBZL)-OSU;Z-L-ASPARTIC ACID BETA-BENZYL-ALPHA-HYDROXYSUCCINIMIDE DIESTER;Z-L-ASPARTIC ACID BETA-BENZYL ESTER ALPHA-N-HYDROXYSUCCINIMIDE ESTER;Z-L-ASPARTIC ACID B-BENZYL-A-HYDROXYSUCCINIMI-DIESTER;CARBOBENZYLOXY-L-ASPARTIC ACID 4-BENZYL 1-(N-HYDROXYSUCCINIMIDE) ESTERS;(3S)-Butanoic Acid 4-[(2,5-Dioxo-1-Pyrrolidinyl)Oxy]-4-Oxo-3-[[(Phenylmethoxy)Carbonyl]Amino]-,Phenylmethyl Ester
• CAS NO: 61464-33-3
• Molecular Formula: C₂₃H₂₂N₂O₈
• Molecular Weight: 454.43
• Mol File: 61464-33-3.mol

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: Z-ASP(OBZL)-OSU(CAS DataBase Reference)
• NIST Chemistry Reference: Z-ASP(OBZL)-OSU(61464-33-3)
• EPA Substance Registry System: Z-ASP(OBZL)-OSU(61464-33-3)

Safety Data

• Hazardous Substances Data: 61464-33-3(Hazardous Substances Data)

Usage

Uses

Used in Biochemistry Research:
Z-ASP(OBZL)-OSU is used as a specific inhibitor of cathepsin B for investigating the enzyme's role in various biological processes and pathological conditions.
Used in Cancer Research:
Z-ASP(OBZL)-OSU is used as a research tool to study the role of cathepsin B in cancer progression, as the enzyme is implicated in tumor growth and metastasis.
Used in Neurodegenerative Disease Research:
Z-ASP(OBZL)-OSU is used as an inhibitor to explore the involvement of cathepsin B in neurodegenerative diseases, where the enzyme may contribute to neuronal damage and cell death.
Used in Other Pathological Condition Research:
Z-ASP(OBZL)-OSU is used to investigate the role of cathepsin B in other pathological conditions where the enzyme's activity may be implicated in disease progression or tissue damage.

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 5872-49-1 L-aspartic acid-α-benzyl ester 
• 2524-64-3 chlorophosphoric acid diphenyl ester 
• 3479-47-8 Z-Asp(OBzl)-OH 

Downstream Products

• 165055-06-1 N-CBZ-β-benzyl-L-aspartyl-D-alanine α-phenylbenzylamide 
• 165055-14-1 N-CBZ-β-benzyl-L-aspartyl-D-phenylglycine (S)-α-methylbenzylamide 
• 165055-07-2 N-CBZ-β-benzyl-L-aspartyl-D-alanine α-(R,S)-cyclopropylbenzylamide 
• 165055-03-8 N-CBZ-β-benzyl-L-aspartyl-D-alanine (R,S)-α-isopropylbenzylamide 
• 165055-18-5 N-CBZ-β-benzyl-L-aspartyl-D-valine (S)-α-ethylbenzylamide 
• 165055-05-0 N-CBZ-β-benzyl-L-aspartyl-D-alanine (R,S)-α-tert-butylbenzylamide 
• 154653-36-8 N-(carbobenzyloxy)-β-benzyl-L-aspartyl-D-α-aminobutyric acid (S)-α-ethylbenzylamide 
• 165055-04-9 N-CBZ-β-benzyl-L-aspartyl-D-alanine (R,S)-α-n-propylbenzylamide 
• 165055-13-0 N-CBZ-β-benzyl-L-aspartyl-D-valine (S)-α-methylbenzylamide 
• 165055-12-9 N-CBZ-β-benzyl-L-aspartyl-D-α-aminopentanoic acid (S)-α-methylbenzylamide 

Relevant articles and documents

Sulfonate derived phosphoramidates as active intermediates in the enzymatic primer-extension of DNA

Novel unnatural 5′-phosphoramidate nucleosides, capable of being processed as substrates by DNA polymerases for multiple nucleotide incorporations, have been designed. The mimics feature metabolites such as taurine and a broad range of aliphatic sulfonates coupled through a P-N bond to the 5′-phosphate position of deoxynucleotides, to allow binding interactions in the enzyme active site. The utility of all of the analogues as pyrophosphate mimics was demonstrated for the chain elongation of DNA, using both thermophilic and mesophilic microbial polymerases. This journal is

Synthesis of non-hydrolyzable substrate analogs for Asp-tRNAAsn/Glu-tRNAGln amidotransferase

Non-hydrolyzable substrate analogs for tRNA-dependent amidotransferase, 2′- or 3′-aspartyl or -glutamyl adenosine, were synthesized from adenosine without protection of the adenine base. The hydroxyl groups of adenosine were selectively protected, followed by a series of oxidation/reductions to alter the stereochemistry. DFT calculations revealed the driving forces for the ketone hydrate formation at C-2′, but not the C-3′ carbon during the oxidation step. Subsequently, triflation and azide replacement yielded azidoadenosines, which were coupled to protected amino acids after deprotection and reduction. After global deprotection, the target substrate analogs were obtained in 2-14% overall yields from adenosine.

Direct PCR amplification of various modified DNAs having amino acids: Convenient preparation of DNA libraries with high-potential activities for in vitro selection

We synthesized modified 2′-deoxyuridine triphosphates bearing amino acids at the C5 position and investigated their substrate properties for KOD Dash DNA polymerase during polymerase chain reaction (PCR). PCR using C5-modified dUTP having an amino acyl group (arginyl, histidyl, lysyl, phenylalanyl, tryptophanyl, leucyl, prolyl, glutaminyl, seryl, O-benzyl seryl or threonyl group) gave the corresponding full-length PCR products in good yield. Although dUTP analogues bearing aspartyl, glutamyl or cysteinyl were found to be poor substrates for PCR catalyzed by KOD Dash DNA polymerase, optimization of the reaction conditions resulted in substantial generation of full-length product. In the case of reaction using dUTP analogue having a cysteinyl group, addition of a reducing agent improved the reaction yield. Thus, PCRs using KOD Dash DNA polymerase together with amino acyl dUTP provide convenient and efficient preparation of various modified DNA libraries with potential protein-like activities.

Process for the preparation of carboxylic acid succinimidyl esters

A process for the preparation of carboxylic acid succinimidyl esters by reaction of N-hydroxysuccinimide with a carboxylic acid and a halophosphoric acid ester of the formula STR1 is desired, in which R1 and R2 are identical or different and are a C2 - to C6 -alkyl radical or a phenyl radical, or R1 and R2 The process is carried out in the presence of a base in a diluent at a temperature of 0° C. up to 100° C. with isolation of the corresponding carboxylic acid succinimidyl ester.

One-pot formation of succinimidyl esters by the system chlorophosphate/hydroxysuccinimide/base

Succinimidyl esters of various carboxylic acids are formed in high yield at ambient to slightly elevated temperature by the system chlorophosphate/hydroxysuccinimide/base.

Discovery and Synthesis of a New Series of High-Potency L-Aspartyl-D-α-aminoalkanoyl-(S)-α-alkylbenzylamide Sweeteners

A new series of L-aspartyl-D-amino acid amide sweeteners is described in which the amide portion is prepared from an α-alkyl-substituted benzylamine.These materials show good taste characteristics and are 5 times more stable than aspartame at typical beve

Structure-taste Relationships of Aspartyl Tripeptide Esters

A series of twenty four analogues of L-α-Asp-Gly-Gly-OMe has been synthesized in relation to structural features of sweet peptides.The rule in the structure-taste relationships of dipeptides is held in the sweet aspartyl tripeptide esters.In order for the