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Key Documents

A3128

Sigma-Aldrich

Ala-Phe

≥98% (TLC)

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About This Item

Formule empirique (notation de Hill):
C12H16N2O3
Numéro CAS:
Poids moléculaire :
236.27
Numéro MDL:
Code UNSPSC :
12352202
ID de substance PubChem :
Nomenclature NACRES :
NA.26

product name

Ala-Phe,

Pureté

≥98% (TLC)

Niveau de qualité

Forme

powder

Couleur

white to off-white

Température de stockage

−20°C

Chaîne SMILES 

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

Clé InChI

OMNVYXHOSHNURL-WPRPVWTQSA-N

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Amino Acid Sequence

Ala-Phe

Actions biochimiques/physiologiques

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.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Yasuhito Shomura et al.
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
Elizabeth A Girnys et al.
Chemical biology & drug design, 75(1), 35-39 (2009-12-04)
Myocardial ischemia and other acute coronary syndromes are leading causes of death worldwide, and often result from a thrombus that blocks an atherosclerotic coronary artery. A key enzyme in thrombus formation is the serine protease thrombin, which is responsible for
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
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

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