Recommended Products
product name
Phe-Ala,
Assay
≥98.0% (TLC)
Quality Level
form
powder
color
white
storage temp.
−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
InChI key
MIDZLCFIAINOQN-WPRPVWTQSA-N
Gene Information
human ... SLC15A1(6564)
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
Certificates of Analysis (COA)
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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
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, 497 ( Pt 3), 773-779 (1996-12-15)
l. Recently two genes have been identified by expression cloning that encode mammalian epithelial peptide transporters capable of translocating di- and tripeptides and selected peptidomimetics by stereoselective and rheogenic substrate-H+ cotransport. PepT1 from rabbit or human small intestine induces a
Biochemistry, 40(14), 4454-4458 (2001-04-04)
This study was initiated to develop inhibitors of the intestinal H(+)/peptide symporter. We provide evidence that the dipeptide derivative Lys[Z(NO(2))]-Pro is an effective competitive inhibitor of mammalian PEPT1 with an apparent binding affinity of 5-10 microM. Characterization of the interaction
Acta crystallographica. Section C, Crystal structure communications, 57(Pt 5), 575-576 (2001-05-16)
A new type of molecular arrangement for dipeptides is observed in the crystal structure of L-phenylalanyl-L-alanine dihydrate, C12H16N2O3-2H2O. Two L-Phe and two L-Ala side chains aggregate into large hydrophobic columns within a three-dimensional hydrogen-bond network.
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