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A1599

Sigma-Aldrich

[des-Arg1]-Angiotensin III

≥95% (HPLC), lyophilized powder

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About This Item

Empirical Formula (Hill Notation):
C40H54N8O8
Molecular Weight:
774.91
MDL number:
MFCD00167496
UNSPSC Code:
12352200

Assay

≥95% (HPLC)

form

lyophilized powder

storage temp.

−20°C

SMILES string

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

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

A1599-BULK:
A1599-5MG:
A1599-VAR:

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Certificates of Analysis (COA)

Lot/Batch Number
105K1152
095K1585
091K1572
024K1102
013K0310

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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
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
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
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
G N Swanson et al.
Regulatory peptides, 40(3), 409-419 (1992-08-13)
We report here the discovery of a unique and novel angiotensin binding site and peptide system based upon the C-terminal 3-8 hexapeptide fragment of angiotensin II (NH3(+)-Val-Tyr-Ile-His-Pro-Phe-COO-) (AII(3-8) (AIV)). This fragment binds saturably, reversibly, specifically, and with high affinity to
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