6610-42-0

Basic information

• Product Name: Z-GLN-GLY-OH
• Synonyms: N-ALPHA-CBZ-GLN-GLY;N-BENZYLOXYCARBONYL-L-GLUTAMINYLGLYCINE;Z-L-GLUTAMINYL-GLYCINE;Z-L-GLUTAMINYL-L-GLYCINE;Z-GLN-GLY;Z-GLN-GLY-OH;BENZYLOXYCARBONYL-L-GLUTAMINYLGLYCINE;na-cbz-gln-gly
• CAS NO: 6610-42-0
• Molecular Formula: C₁₅H₁₉N₃O₆
• Molecular Weight: 337.33
• Product Categories: Dipeptides;Dipeptides and Tripeptides;Peptides
• Mol File: 6610-42-0.mol

Chemical Properties

• Boiling Point: 748°Cat760mmHg
• Flash Point: 406.2°C
• Appearance: /Solid
• Density: 1.339
• Vapor Pressure: 1.67E-23mmHg at 25°C
• Refractive Index: 1.567
• Storage Temp.: −20°C
• Solubility: Chloroform (Slightly, Sonicated) Methanol (Slightly), Water (Slightly, Sonicated
• PKA: 3.38±0.10(Predicted)
• CAS DataBase Reference: Z-GLN-GLY-OH(CAS DataBase Reference)
• NIST Chemistry Reference: Z-GLN-GLY-OH(6610-42-0)
• EPA Substance Registry System: Z-GLN-GLY-OH(6610-42-0)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 6610-42-0(Hazardous Substances Data)

Usage

Uses

Used in Enzyme Activity Assays:
Z-GLN-GLY-OH is used as a γ-glutamyl donor substrate for the spectrophotometric determination of transglutaminase (TGase) activity. This application helps researchers evaluate the functionality and efficiency of TGase enzymes in various experimental setups.
Used in Biochemistry Research:
In the field of biochemistry, Z-GLN-GLY-OH is used as a substrate for enzymatic synthesis of N-linked neoglycoproteins. This process allows scientists to study the role of glycoproteins in cellular processes and develop potential therapeutic agents targeting glycoprotein-related diseases.

Biochem/physiol Actions

N-Benzyloxycarbonyl-L-Glutaminylglycine (Z-Gln-Gly, Z-QG) is used as a substrate to differentiate and characterize transglutaminase(s) (TGase) that catalyzes the post-translational covalent cross-linking of Gln- and Lys-containing peptides. Z-QG supports glutamyl-level cross-linking applications thruough surface modification.

InChI:InChI=1/C15H19N3O6/c16-12(19)7-6-11(14(22)17-8-13(20)21)18-15(23)24-9-10-4-2-1-3-5-10/h1-5,11H,6-9H2,(H2,16,19)(H,17,22)(H,18,23)(H,20,21)

Upstream product

• 35726-62-6 (S)-2-(benzyloxycarbonylamino)-5-ethoxy-5-oxopentanoic acid 
• 45171-75-3 N-(O-ethyl-L-α-glutamyl)-glycine 
• 4587-40-0 N-(N-benzyloxycarbonyl-α-L-glutamyl)-glycine ethyl ester 
• 2650-64-8 Cbz-L-Gln 
• 7763-16-8 N²-benzyloxycarbonyl-L-glutamine-(4-nitro-phenyl ester) 
• 56-40-6 glycine 
• 7750-54-1 N-(O-ethyl-N-benzyloxycarbonyl-L-α-glutamyl)-glycine 
• 2731-88-6 Z-Gln-Gly-OEt 

Downstream Products

• 127290-82-8 Cbz-L-Gln-Gly-Gly 
• 1332848-71-1 5-[3-(Z-Gln-Gly-amido)-1-(E)-propenyl]-2'-deoxyuridine-5'-triphosphate 
• 67964-58-3 Z-α-L-Glutamyl-(γ-hydrazid)-glycin 
• 861855-48-3 [4-(3-amino-2-hydroxy-propylcarbamoyl)-2-benzyloxycarbonylamino-butyrylamino]-acetic acid 

Relevant articles and documents

Peptide coupling of unprotected amino acids through in situ p-nitrophenyl ester formation

Several series of dipeptides and tripeptides were prepared via an activation-coupling method involving the in situ formation of a p-nitrophenyl ester of an (N-protected) amino acid, followed by coupling with an unprotected amino acid in partially aqueous solutions. The resulting peptide is easily isolated by precipitation. In general, the yields obtained are good to excellent and racemization is minimal. This method is particularly advantageous with respect to its simplicity and lack of obligatory side chain protection/deprotection steps.