A1599
[des-Arg1]-Angiotensin III
≥95% (HPLC), lyophilized powder
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About This Item
Fórmula empírica (Notação de Hill):
C40H54N8O8
Peso molecular:
774.91
Número MDL:
Código UNSPSC:
12352200
Ensaio
≥95% (HPLC)
forma
lyophilized powder
temperatura de armazenamento
−20°C
cadeia de caracteres SMILES
CC[C@H](C)[C@H](NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@@H](N)C(C)C)C(=O)N[C@@H](Cc2c[nH]cn2)C(=O)N3CCC[C@H]3C(=O)N[C@@H](Cc4ccccc4)C(O)=O
Código de classe de armazenamento
13 - Non Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
Certificados de análise (COA)
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Hanna Andersson et al.
Journal of medicinal chemistry, 54(11), 3779-3792 (2011-04-12)
Macrocyclic analogues of angiotensin IV (Ang IV, Val(1)-Tyr(2)-Ile(3)-His(4)-Pro(5)-Phe(6)) targeting the insulin-regulated aminopeptidase (IRAP) have been designed, synthesized, and evaluated biologically. Replacement of His(4)-Pro(5)-Phe(6) by a 2-(aminomethyl)phenylacetic acid (AMPAA) moiety and of Val(1) and Ile(3) by amino acids bearing olefinic side
Aneta Lukaszuk et al.
Journal of medicinal chemistry, 51(7), 2291-2296 (2008-04-05)
Angiotensin IV, a metabolite of angiotensin II, inhibits the enzyme insulin regulated aminopeptidase or IRAP and also, although with lower potency, aminopeptidase-N (AP-N). When both beta (2)-homo amino acid- and beta (3)-homo amino acid substitutions were used, allowed the identification
Hanna Andersson et al.
Bioorganic & medicinal chemistry, 16(14), 6924-6935 (2008-06-17)
Analogues of the hexapeptide angiotensin IV (Ang IV, Val(1)-Tyr(2)-Ile(3)-His(4)-Pro(5)-Phe(6)) encompassing a 4-hydroxydiphenylmethane scaffold replacing Tyr(2) and a phenylacetic or benzoic acid moiety replacing His(4)-Pro(5)-Phe(6) have been synthesized and evaluated in biological assays. The analogues inhibited the proteolytic activity of cystinyl
K Hermann et al.
Journal of neurochemistry, 52(3), 863-868 (1989-03-01)
The degradation pattern and rate of [Ile5]-Angiotensin (Ang) I, II, and III were studied in neuron-enriched and glia-enriched cells in primary cultures from rat brain. Metabolites were separated by HPLC, and their identities were evaluated by comparison of their retention
Aneta Lukaszuk et al.
Journal of medicinal chemistry, 52(18), 5612-5618 (2009-09-18)
The histidine residue in angiotensin IV was replaced by various conformationally constrained amino acids. The substitution of the His(4)-Pro(5) dipeptide sequence by the constrained Trp analogue Aia-Gly, in combination with beta(2)hVal substitution at the N-terminus, provided a new stable analogue
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