470058
D-Tyrosinol hydrochloride
98%
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About This Item
Linear Formula:
4-(HO)C6H4CH2CH(NH2)CH2OH · HCl
CAS Number:
Molecular Weight:
203.67
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.22
Quality Level
Assay
98%
optical activity
[α]22/D +18°, c = 1 in H2O
reaction suitability
reaction type: solution phase peptide synthesis
mp
161-165 °C (lit.)
application(s)
peptide synthesis
SMILES string
Cl[H].N[C@@H](CO)Cc1ccc(O)cc1
InChI
1S/C9H13NO2.ClH/c10-8(6-11)5-7-1-3-9(12)4-2-7;/h1-4,8,11-12H,5-6,10H2;1H/t8-;/m1./s1
InChI key
PNGCRFWYSRUQTB-DDWIOCJRSA-N
Related Categories
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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E M Newman et al.
Cancer research, 43(10), 4703-4708 (1983-10-01)
The effects of amino acid deprivation and treatment with amino alcohols upon the growth, viability, and susceptibility to methotrexate (MTX) cytotoxicity were examined in BALB/3T3 cells and their virally transformed counterparts, SV-T2 cells. Cells were deprived of either histidine or
Eric T Larson et al.
Journal of molecular biology, 409(2), 159-176 (2011-03-23)
The single tyrosyl-tRNA synthetase (TyrRS) gene in trypanosomatid genomes codes for a protein that is twice the length of TyrRS from virtually all other organisms. Each half of the double-length TyrRS contains a catalytic domain and an anticodon-binding domain; however
C Monteilhet et al.
Journal of molecular biology, 173(4), 477-485 (1984-03-15)
Crystalline complexes of tyrosyl-tRNA synthetase from Bacillus stearothermophilus were prepared with adenosine, AMP, ATP and PPi, all in the presence of tyrosinol, which binds strongly to the tyrosine binding site but cannot be adenylated by ATP. The hydrolysis of ATP
M Angeles Gilabert et al.
Biological chemistry, 385(12), 1177-1184 (2005-01-18)
We report here on the stereospecificity observed in the action of horseradish peroxidase (HRPC) on monophenol and diphenol substrates. Several enantiomers of monophenols and o-diphenols were assayed: L-tyrosinol, D-tyrosinol, L-tyrosine, DL-tyrosine, D-tyrosine, L-dopa, DL-dopa, D-dopa, L-alpha-methyldopa, DL-alpha-methyldopa, DL-adrenaline, D-adrenaline, L-isoproterenol
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