| Identification | Back Directory | [Name]
ASP-ARG-VAL-TYR-ILE-HIS-PRO-PHE-HIS-LEU-VAL-ILE-HIS-ASN | [CAS]
104180-23-6 | [Synonyms]
DRVYIHPFHLVIHN
RENIN SUBSTRATE
ANGIOTENSINOGEN
Tetradecapeptid
H-DRVYIHPFHLVIHN-OH
ANGIOTENSINOGEN 1-14
ANGIOTENSIN PRECURSOR
RENIN SUBSTRATE, HUMAN
PREANGIOTENSINOGEN 1-14
HUMAN PREANGIOTENSINOGEN 1-14
ANGIOTENSINOGEN FRAGMENT 1-14
ANGIOTENSINOGEN (1-14) (HUMAN)
RENIN SUBSTRATE TETRADECAPEPTIDE
PREANGIOTENSINOGEN (1-14) (HUMAN)
RENIN SUBSTRATE TETRADECAPEPTIDE HUMAN
TETRADECAPEPTIDE RENIN SUBSTRATE (HUMAN)
ASP-ARG-VAL-TYR-ILE-HIS-PRO-PHE-HIS-LEU-VAL-ILE-HIS-ASN
Renin Substrate Tetradecapeptide Porcine acetate salt
ASP-ARG-VAL-TYR-ILE-HIS-PRO-PHE-HIS-LEU-VAL-ILE-HIS-ASN-OH
H-ASP-ARG-VAL-TYR-ILE-HIS-PRO-PHE-HIS-LEU-VAL-ILE-HIS-ASN-OH
Angiotensinogen 1-14, Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Asn
Angiotensinogen (1-14) (huMan), Tetradecapeptide Renin Substrate (huMan), Preangiotensinogen (1-14) (huMan)
L-Asparagine, L-α-aspartyl-L-arginyl-L-valyl-L-tyrosyl-L-isoleucyl-L-histidyl-L-prolyl-L-phenylalanyl-L-histidyl-L-leucyl-L-valyl-L-isoleucyl-L-histidyl- | [Molecular Formula]
C83H122N24O19 | [MDL Number]
MFCD00151759 | [MOL File]
104180-23-6.mol | [Molecular Weight]
1760.01 |
| Chemical Properties | Back Directory | [storage temp. ]
−20°C
| [form ]
lyophilized powder
| [color ]
White to off-white | [Water Solubility ]
Soluble in Water | [Sequence]
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Asn |
| Hazard Information | Back Directory | [Uses]
Angiotensinogen (1-14), human is a fragment of the renin substrate angiotensinogen. Angiotensinogen is naturally occurring substrate for renin and a precursor for all angiotensin peptides[1][2]. | [IC 50]
Human Endogenous Metabolite | [References]
[1] Lu H, et al. Structure and functions of angiotensinogen. Hypertens Res. 2016 Jul;39(7):492-500. DOI:10.1038/hr.2016.17
[2] Burton J, et al. The amino-acid residues on the C-terminal side of the cleavage site of angiotensinogeninfluence the species specificity of reaction with renin. iochim Biophys Acta. 1988 Jan 4;952(1):8-12. DOI:10.1016/0167-4838(88)90095-7 |
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