A3128
Ala-Phe
≥98% (TLC)
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About This Item
Fórmula empírica (notación de Hill):
C12H16N2O3
Número de CAS:
Peso molecular:
236.27
MDL number:
UNSPSC Code:
12352202
PubChem Substance ID:
NACRES:
NA.26
Productos recomendados
Nombre del producto
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
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Kyung Min Choi et al.
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
Zhi-Xia Zheng et al.
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
Xiao-Lin Zhu et al.
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
Tomasz Pawlak et al.
The journal of physical chemistry. B, 116(6), 1974-1983 (2012-01-14)
DFT methods were employed to compute the (13)C NMR chemical shift tensor (CST) parameters for crystals of YAF peptides (Tyr-Ala-Phe) with different stereochemistry for the Ala residue. Tyr-D-Ala-Phe 1 crystallizes in the C2 space group while Tyr-L-Ala-Phe crystallizes in either
J Li et al.
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
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