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Product Name
Ala-Phe,
Assay
≥98% (TLC)
Quality Level
form
powder
color
white to off-white
storage temp.
−20°C
SMILES string
C[C@H](N)C(=O)N[C@@H](Cc1ccccc1)C(O)=O
InChI
1S/C12H16N2O3/c1-8(13)11(15)14-10(12(16)17)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
OMNVYXHOSHNURL-WPRPVWTQSA-N
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Amino Acid Sequence
Ala-Phe
Biochem/physiol Actions
Alanyl dipeptides such as ala-leu, ala-lys, ala-gly, ala-pro, ala-tyr and ala-phe may be used in physicochemical studies or to evaluate dipeptide separation technologies. Alanyl dipeptides may also be used for studying cell uptake mechanisms, dipeptide metabolism or cell growth supplementation benefits.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Journal of agricultural and food chemistry, 55(21), 8367-8371 (2007-10-12)
A replicate heart-cut column-switching HPLC method combined with two switching valves was newly developed for the simultaneous determination of three antihypertensive peptides (Ala-Phe, Tyr-Pro, and Trp-Tyr) in tryptic casein hydrolysate in one run-in assay. After a first separation on an
Electrophoresis, 26(4-5), 1007-1012 (2005-02-17)
A ligand-exchange capillary electrophoresis was explored, with L-ornithine as the ligand and copper(II) as the central ion. Its applicability was demonstrated with underivatized and dansyl amino acids, a dipeptide, and drugs with amino alcohol structure. The enantioselectivity was found to
Electrophoresis, 20(1), 171-179 (1999-03-05)
The separation of stereoisomers, particularly enantiomers, is important when their physiological activity differs. We have resolved the four stereoisomers each of alanylphenylalanine (Ala-Phe) and of leucylphenylalanine (Leu-Phe) by capillary electrophoresis using beta-cyclodextrin as a buffer additive and urea to enhance
Analytical biochemistry, 367(2), 167-172 (2007-06-30)
A spectrophotometric assay to determine peptide transport has been developed. Using two chromogenic peptide mimetics, L-phenylalanyl-L-2-sulfanilylglycine (PSG) and L-phenylalanyl-L-3-thiaphenylalanine (PSP), the peptide transport patterns in individual cell species can be evaluated effectively. After the addition of PSG to a HeLa
Protein science : a publication of the Protein Society, 21(5), 707-716 (2012-03-13)
BacD is an ATP-dependent dipeptide ligase responsible for the biosynthesis of L-alanyl-L-anticapsin, a precursor of an antibiotic produced by Bacillus spp. In contrast to the well-studied and phylogenetically related D-alanine: D-alanine ligase (Ddl), BacD synthesizes dipeptides using L-amino acids as
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