| Identification | Back Directory | [Name]
Z-PHE-LEU-GLU-PNA | [CAS]
104634-10-8 | [Synonyms]
Z-FLE-PNA
Z-PHE-LEU-GLU-PNA
L-α-Glutamine, N-[(phenylmethoxy)carbonyl]-L-phenylalanyl-L-leucyl-N-(4-nitrophenyl)-
(4S)-4-[[(2S)-4-methyl-2-[[(2S)-3-phenyl-2-(phenylmethoxycarbonylamino)propanoyl]amino]pentanoyl]amino]-5-(4-nitroanilino)-5-oxopentanoic acid | [Molecular Formula]
C34H39N5O9 | [MDL Number]
MFCD01940686 | [MOL File]
104634-10-8.mol | [Molecular Weight]
661.7 |
| Chemical Properties | Back Directory | [Boiling point ]
1004.4±65.0 °C(Predicted) | [density ]
1.304±0.06 g/cm3(Predicted) | [form ]
Solid | [pka]
4.42±0.10(Predicted) | [color ]
White to off-white | [Sequence]
Z-Phe-Leu-{Glu-pNA} |
| Hazard Information | Back Directory | [Uses]
Z-Phe-Leu-Glu-pNA is a chromogenic substrate for glutamyl endopeptidases. Z-Phe-Leu-Glu-pNA has been used as a synthetic substrate in the study of proteolytic enzymes, including trypsin treatment, subtilisin and chymotrypsin. Z-Phe-Leu-Glu-pNA plays an important role in hormone disorders such as prostate cancer and breast cancer[1][2]. | [References]
[1] Wei Ye, et al. Characterization of the glutamate-specific endopeptidase from?Bacillus licheniformis?expressed in?Escherichia coli. J Biotechnol. 2013 Oct 10;168(1):40-5. DOI:10.1016/j.jbiotec.2013.08.009
[2] Wei Ye, et al. A new strategy for recovery of two peptides without Glu employing glutamate-specific endopeptidase from Bacillus licheniformis. Enzyme Microb Technol. 2014 Jan 10:54:25-31. DOI:10.1016/j.enzmictec.2013.09.013 |
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