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18055

Sigma-Aldrich

4-Bromo-L-phenylalanine

≥98.0% (NT)

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About This Item

Empirical Formula (Hill Notation):
C9H10BrNO2
CAS Number:
Molecular Weight:
244.09
Beilstein:
2212159
MDL number:
UNSPSC Code:
12352200
PubChem Substance ID:
NACRES:
NA.22

Assay

≥98.0% (NT)

form

solid

optical activity

[α]20/D −22.0±2°, c = 0.5% in H2O

reaction suitability

reaction type: solution phase peptide synthesis

mp

~265 °C (dec.)

application(s)

peptide synthesis

SMILES string

N[C@@H](Cc1ccc(Br)cc1)C(O)=O

InChI

1S/C9H10BrNO2/c10-7-3-1-6(2-4-7)5-8(11)9(12)13/h1-4,8H,5,11H2,(H,12,13)/t8-/m0/s1

InChI key

PEMUHKUIQHFMTH-QMMMGPOBSA-N

Pictograms

Skull and crossbones

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Acute Tox. 3 Oral

Storage Class Code

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

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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Neutron capture therapy for melanoma.
J A Coderre et al.
Basic life sciences, 50, 219-232 (1989-01-01)
Thermal neutron capture therapy: the Japanese-Australian clinical trial for malignant melanoma.
B J Allen et al.
Basic life sciences, 50, 69-73 (1989-01-01)
Inchan Kwon et al.
Journal of the American Chemical Society, 128(36), 11778-11783 (2006-09-07)
Introduction of a yeast suppressor tRNA (ytRNA(Phe)(CUA)) and a mutant yeast phenylalanyl-tRNA synthetase (yPheRS (T415G)) into an Escherichia coli expression host allows in vivo incorporation of phenylalanine analogues into recombinant proteins in response to amber stop codons. However, high-fidelity incorporation
Dose fractionation in neutron capture therapy for malignant melanoma.
B J Allen et al.
Basic life sciences, 50, 63-67 (1989-01-01)
M Ibba et al.
FEBS letters, 364(3), 272-275 (1995-05-15)
It has previously been demonstrated that the unnatural amino acid p-Cl-phenylalanine can be attached to tRNA(Phe) by a modified phenylalanyl-tRNA synthetase with relaxed amino acid substrate specificity. We show that this modification to the translational machinery of Escherichia coli is

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