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Product Information

Product Name
Z-L-tyrosine 4-nitrophenyl ester
Brand Name
Chem Impex
Product Number
02268
CAS
3556-56-7
Certificate of Analysis (COA)​
COA not found

General Information

PubChem CID
11102156
IUPAC Name
(4-nitrophenyl) (2S)-3-(4-hydroxyphenyl)-2-(phenylmethoxycarbonylamino)propanoate
InChI Key
WUHIFOXZYIQZFP-NRFANRHFSA-N
SMILES
C1=CC=C(C=C1)COC(=O)NC@@H(CC2=CC=C(C=C2)O)C(=O)OC3=CC=C(C=C3)N+(=O)O-

Application

Z-L-tyrosine 4-nitrophenyl ester is widely utilized in research focused on:

Biochemical Research: This compound serves as a substrate in enzyme assays, helping researchers study the activity of various enzymes involved in metabolic pathways.

Drug Development: Its properties make it a valuable intermediate in synthesizing pharmaceuticals, particularly those targeting neurological disorders due to its structural similarity to neurotransmitters.

Protein Engineering: Used in the modification of proteins, this ester can enhance the solubility and stability of therapeutic proteins, improving their efficacy in medical applications.

Analytical Chemistry: It acts as a standard in chromatographic techniques, allowing for the accurate quantification of tyrosine derivatives in complex biological samples.

Cosmetic Formulations: The compound is incorporated into skincare products for its antioxidant properties, contributing to formulations aimed at reducing oxidative stress on the skin.

References Data Source From Pubchem

Substarte Specificty and Immobilization Studies of Purified Solanain from the Latex of Vallaris solanacea

Publication Name: International Journal of Peptide Research and Therapeutics
Publication Date: 2017-12-04
DOI: 10.1007/s10989-017-9659-4

Characterization of Codon-Optimized Recombinant Candida rugosa Lipase 5 (LIP5)

Publication Name: Journal of Agricultural and Food Chemistry
Publication Date: 2011-09-14
DOI: 10.1021/jf202161a

Enzyme Kinetics: Stopped-Flow Under Extreme Conditions

Publication Name: Biological Systems Under Extreme Conditions
Publication Date: 2002
DOI: 10.1007/978-3-662-04802-3_8

C‐terminal His‐tagging results in substrate specificity changes of the thioesterase I from Escherichia coli

Publication Name: Journal of the American Oil Chemists’ Society
Publication Date: 1999-10
DOI: 10.1007/s11746-999-0082-7

High Hydrostatic Pressure and Enzymology

Publication Name: High Pressure Molecular Science
Publication Date: 1999
DOI: 10.1007/978-94-011-4669-2_22