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857246

Sigma-Aldrich

p-Bromo-DL-phenylalanine

99%

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About This Item

Linear Formula:
BrC6H4CH2CH(NH2)CO2H
CAS Number:
Molecular Weight:
244.09
EC Number:
MDL number:
UNSPSC Code:
12352209
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.22

Assay

99%

form

powder

reaction suitability

reaction type: solution phase peptide synthesis

mp

262-263 °C (dec.) (lit.)

application(s)

peptide synthesis

storage temp.

2-8°C

SMILES string

NC(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)

InChI key

PEMUHKUIQHFMTH-UHFFFAOYSA-N

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Pictograms

Exclamation mark

Signal Word

Warning

Hazard 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


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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)
James M Turner et al.
Proceedings of the National Academy of Sciences of the United States of America, 103(17), 6483-6488 (2006-04-19)
Recently, tRNA aminoacyl-tRNA synthetase pairs have been evolved that allow one to genetically encode a large array of unnatural amino acids in both prokaryotic and eukaryotic organisms. We have determined the crystal structures of two substrate-bound Methanococcus jannaschii tyrosyl aminoacyl-tRNA
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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