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P3251
Phe-Ala
≥98.0% (TLC)
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About This Item
Empfohlene Produkte
Produktbezeichnung
Phe-Ala,
Assay
≥98.0% (TLC)
Qualitätsniveau
Form
powder
Farbe
white
Lagertemp.
−20°C
SMILES String
C[C@H](NC(=O)[C@@H](N)Cc1ccccc1)C(O)=O
InChI
1S/C12H16N2O3/c1-8(12(16)17)14-11(15)10(13)7-9-5-3-2-4-6-9/h2-6,8,10H,7,13H2,1H3,(H,14,15)(H,16,17)/t8-,10-/m0/s1
InChIKey
MIDZLCFIAINOQN-WPRPVWTQSA-N
Angaben zum Gen
human ... SLC15A1(6564)
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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Peptides, 17(1), 31-37 (1996-01-01)
The purpose of present study was to determine whether peptidase activity affects the release of substance P (SP) and calcitonin gene-related peptide (CGRP) from spinal cord slices. When slices were exposed to various inhibitors of endopeptidase 24.11, the resting and
The Journal of physiology, 516 ( Pt 1), 209-217 (1999-03-06)
1. The spatial and temporal distribution of intracellular H+ ions in response to activation of a proton-coupled dipeptide transporter localized at the apical pole of mouse small intestinal isolated enterocytes was investigated using intracellular carboxy-SNARF-1 fluorescence in combination with whole-cell
The Journal of experimental biology, 203(Pt 19), 2991-3001 (2000-09-08)
H(+)/peptide cotransport in brush-border membrane vesicles (BBMVs) from eel (Anguilla anguilla) intestine was studied by measuring d-[(3)H]-phenylalanyl-l-alanine uptake and by monitoring peptide-dependent intravesicular acidification using the pH-sensitive dye Acridine Orange. d-[(3)H]-phenylalanyl-l-alanine influx was greatly stimulated by an inside-negative membrane potential
Physical chemistry chemical physics : PCCP, 12(41), 13383-13393 (2010-09-08)
Electrospray ionization produces phenylalanine (Phe) complexes of the alkali metal ion series, plus Ag(+) and Ba(2+). Infrared multiple photon dissociation (IRMPD) spectroscopy using the FELIX free electron laser light source is used to characterize the conformations of the ions, in
The American journal of physiology, 275(6 Pt 1), C1573-C1579 (1998-12-09)
The reabsorption of filtered di- and tripeptides as well as certain peptide mimetics from the tubular lumen into renal epithelial cells is mediated by an H+-coupled high-affinity transport process. Here we demonstrate for the first time H+-coupled uptake of dipeptides
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