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Merck

A4316

Sigma-Aldrich

Anantin from Streptomyces coerulescens

≥90% (HPLC)

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About This Item

Fórmula empírica (notación de Hill):
C90H111N21O24
Número de CAS:
Peso molecular:
1870.97
MDL number:
UNSPSC Code:
12352200

assay

≥90% (HPLC)

storage temp.

−20°C

Amino Acid Sequence

Cyclo(Gly-Phe-Ile-Gly-Trp-Gly-Asn-β-Asp)-Ile-Phe-Gly-His-Tyr-Ser-Gly-Asp-Phe

Biochem/physiol Actions

Competitive antagonist at atrial natriuretic peptide NPR-A receptors.

Other Notes

A cyclic peptide

Storage Class

13 - Non Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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D F Wyss et al.
The Journal of antibiotics, 44(2), 172-180 (1991-02-01)
Anantin, a naturally occurring peptide from Streptomyces coerulescens, binds competitively to the receptor of atrial natriuretic factor (ANF) from bovine adrenal cortex (Kd = 0.6 microM) and acts as ANF antagonist. Protein chemical data and FAB-MS have identified anantin to
Rouwayda El-Ayoubi et al.
British journal of pharmacology, 145(1), 50-56 (2005-02-09)
We have previously shown that acute intravenous injections of moxonidine and clonidine increase plasma atrial natriuretic peptide (ANP), a vasodilator, diuretic and natriuretic hormone. We hypothesized that moxonidine stimulates the release of ANP, which would act on its renal receptors
Sandra L Hrometz et al.
Toxicology letters, 206(2), 234-237 (2011-08-11)
MDMA (3,4-methylenedioxymethamphetamine) induces thermogenesis in a mitochondrial uncoupling protein 3-dependent manner. There is evidence that this hyperthermia is mediated in part by the lipolytic release of free fatty acids, that subsequently activate uncoupling protein 3 in skeletal muscle mitochondria. We
S Nachshon et al.
The American journal of physiology, 268(3 Pt 1), E428-E432 (1995-03-01)
Atrial natriuretic peptide (ANP) is a hormone-secreted predominantly by atrial myocytes. ANP exerts many of its actions via activation of the particulate guanylyl cyclase receptor ANPR-A and the formation of guanosine 3',5'-cyclic monophosphate (cGMP), which serves as a second messenger
Martin Kerr et al.
Current biology : CB, 14(16), 1468-1474 (2004-08-25)
Every living cell must detect, and respond appropriately to, external signals. The functions of intracellular second messengers, such as guanosine 3'5'-cyclic monophosphate (cGMP), adenosine 3'5'-cyclic monophosphate (cAMP), and intracellular calcium, are thus intensively studied. However, artifact-free manipulation of these messengers

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