InChI
1S/C11H13NO4/c1-7(13)12-10(11(15)16)6-8-2-4-9(14)5-3-8/h2-5,10,14H,6H2,1H3,(H,12,13)(H,15,16)/t10-/m0/s1
InChI key
CAHKINHBCWCHCF-JTQLQIEISA-N
SMILES string
CC(=O)N[C@@H](Cc1ccc(O)cc1)C(O)=O
biological source
non-animal source
assay
≥98.5%
form
crystalline powder
manufacturer/tradename
Ajinomoto
technique(s)
cell culture | mammalian: suitable
impurities
endotoxin, heavy metals, tested
solubility
H2O: 25 mg/mL
application(s)
pharmaceutical (small molecule)
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General description
To request documentation for this product, please contact Customer Support and select ‘Product Documentation′. Please note that access to documentation for this product requires a confidentiality disclosure agreement.
Application
L-Tyrosine is a non-essential amino acid. It can be used as a cell culture media component in the commercial biomanufacture of therapeutic recombinant proteins and monoclonal antibodies. N-Acetyl-L-tyrosine is an acetylated derivative of the essential amino acid L-tyrosine with reported improved nutritional properties.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Investigation of DNA-protein cross-link formation between lysozyme and oxanine by mass spectrometry.
Hauh-Jyun Candy Chen et al.
Chembiochem : a European journal of chemical biology, 9(7), 1074-1081 (2008-03-21)
Reactive nitrogen species are implicated in inflammatory diseases and cancers. Oxanine (Oxa) is a DNA lesion product originating from the guanine base through exposure to nitric oxide, nitrous acid, or N-nitrosoindoles. Oxanine was found to mediate formation of DNA-protein cross-links
Michael J Napolitano et al.
Chemical research in toxicology, 18(3), 501-508 (2005-03-22)
The reactions of aqueous ClO2 with tyrosine, N-acetyltyrosine, and dopa (3,4-dihydroxyphenylalanine) are investigated from pH 4 to 7. The reaction rates increase greatly with pH to give a series of oxidized products. Tyrosine and N-acetyltyrosine have similar reactivities with second-order
A Rescigno et al.
Biochimica et biophysica acta, 1384(2), 268-276 (1998-07-11)
Tyrosinase is a copper containing protein which catalyzes the hydroxylation of monophenols and the oxidation of diphenols to o-quinones. The monophenolase activity of tyrosinase is characterized by a typical lag time. In this paper the influence of 3-hydroxyanthranilic acid on
G Drabik et al.
Acta biochimica Polonica, 48(1), 271-275 (2001-07-07)
N-acetyl-L-tyrosine (N-acTyr), with the alpha amine residue blocked by acetylation, can mimic the reactivity of exposed tyrosyl residues incorporated into polypeptides. In this study chlorination of N-acTyr residue at positions 3 and 5 in reactions with NaOCl, chloramines and the
M Lehnig
Archives of biochemistry and biophysics, 393(2), 245-254 (2001-09-15)
During reaction of N-acetyl-l-tyrosine with the nitrating system (15)NO(-)(2)/H(2)O(2)/HRP at pH 7.5, emission is observed in the (15)N NMR signals of 3-nitro-N-acetyl-l-tyrosine and the 1-nitrocyclohexa-2,5-dien-4-one derivative of N-acetyl-l-tyrosine. The occurrence of (15)N CIDNP proves the formation of radical pairs. The
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