V5626
Val-Tyr
>98% (TLC), suitable for ligand binding assays
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About This Item
Fórmula empírica (notación de Hill):
C14H20N2O4
Número de CAS:
Peso molecular:
280.32
Número MDL:
Código UNSPSC:
12352200
ID de la sustancia en PubChem:
NACRES:
NA.26
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Nombre del producto
Val-Tyr,
Ensayo
>98% (TLC)
Formulario
powder
técnicas
ligand binding assay: suitable
color
white to off-white
temp. de almacenamiento
−20°C
cadena SMILES
OC([C@@H](NC([C@@H](N)C(C)C)=O)CC1=CC=C(O)C=C1)=O
InChI
1S/C14H20N2O4/c1-8(2)12(15)13(18)16-11(14(19)20)7-9-3-5-10(17)6-4-9/h3-6,8,11-12,17H,7,15H2,1-2H3,(H,16,18)(H,19,20)
Clave InChI
VEYJKJORLPYVLO-UHFFFAOYSA-N
Código de clase de almacenamiento
13 - Non Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, type N95 (US)
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Jocksan I Morales-Camacho et al.
Applied microbiology and biotechnology (2018-09-14)
The insertion of peptides is a biotechnology tool widely used to improve the nutraceutical properties of proteins. Because the effect of these insertions in protein stability and function is difficult to predict, it should be determined experimentally. In this study
Mitsuru Tanaka et al.
Bioscience, biotechnology, and biochemistry, 70(9), 2292-2295 (2006-09-09)
In this study, we found that antihypertensive di-peptide Val-Tyr (VY) showed a vascular relaxation effect in KCl-induced contraction of thoracic aorta rings from 18-week-old spontaneously hypertensive rats among di-peptides of VY, Ile-Tyr, and Tyr-Val irrespective of their angiotensin I-converting enzyme
Takao Ueno et al.
Analytical sciences : the international journal of the Japan Society for Analytical Chemistry, 21(8), 997-1000 (2005-08-27)
A double column-switching HPLC method with naphthalene-2,3-dialdehyde (NDA) was applied for determination of two plasma antihypertensive peptides, Val-Tyr (VY) and Ile-Val-Tyr (IVY). After a first separation on a Phe-ODS column, double heart-cuts of the retention time corresponding to NDA-VY and
Mitsuru Tanaka et al.
Scientific reports, 9(1), 5769-5769 (2019-04-10)
Apart from nutrients required for the brain, there has been no report that naturally occurring peptides can cross the blood-brain barrier (BBB). The aim of this study was to identify the BBB-transportable peptides using in situ mouse perfusion experiments. Based
Lieselot Vercruysse et al.
Peptides, 29(2), 261-267 (2008-01-29)
Antihypertensive peptides received much interest over the last decade. These peptides are known to be angiotensin converting enzyme (ACE) inhibitors in vitro, but the actual antihypertensive mechanisms in vivo are still unclear. In this research, we used rat aortic rings
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