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Adrenomedullin (1-12), human Sale

(Synonyms: H2N-Tyr-Arg-Gln-Ser-Met-Asn-Asn-Phe-Gln-Gly-Leu-Arg-OH ) 目录号 : GP10113

An N-terminal fragment of adrenomedullin

Adrenomedullin (1-12), human Chemical Structure

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5mg
¥347.00
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10mg
¥557.00
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25mg
¥756.00
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产品描述

Adrenomedullin (AM) (1-12), human (C64H100N22O19S1), is a peptide with the sequence Tyr-Arg-Gln-Ser-Met-Asn-Asn-Phe-Gln-Gly-Leu-Arg. It was first discovered to be associated with pheochromocytoma, a tumor arising from adrenal medulla, in 1993. AM was initially identified as a vasodilator, and as such, it has the ability to relax vascular tone. Previous research cited it as the most potent endogenous vasodilatory peptide found in the body. Other effects of AM include the increase of cell tolerance to oxidative stress and hypoxic injury and angiogenesis. AM is seen as a positive influence in diseases such as hypertension, myocardial infarction, chronic obstructive pulmonary disease and other cardiovascular conditions.

Chemical Properties

Cas No. SDF
别名 H2N-Tyr-Arg-Gln-Ser-Met-Asn-Asn-Phe-Gln-Gly-Leu-Arg-OH
Canonical SMILES N[C@@H](CC1=CC=C(O)C=C1)C(N[C@@H](CCCNC(N)=N)C(N[C@@H](CCC(N)=O)C(N[C@@H](CO)C(N[C@@H](CCSC)C(N[C@@H](CC(N)=O)C(N[C@@H](CC(N)=O)C(N[C@@H](CC2=CC=CC=C2)C(N[C@@H](CCC(N)=O)C(NCC(N[C@@H](CC(C)C)C(N[C@@H](CCCNC(N)=N)C(O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O
分子式 C64H100N22O19S 分子量 1513.68
溶解度 ≥ 151.3mg/mL in DMSO 储存条件 Store at -20°C
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溶解性数据

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1 mM 0.6606 mL 3.3032 mL 6.6064 mL
5 mM 0.1321 mL 0.6606 mL 1.3213 mL
10 mM 0.0661 mL 0.3303 mL 0.6606 mL
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Research Update

Specific adrenomedullin binding sites in the human brain

Binding sites for adrenomedullin in human brain were investigated and characterized by radioligand binding. Specific binding sites for adrenomedullin were present in every region of human brain (cerebral cortex, cerebellum, thalamus, hypothalamus, pons and medulla oblongata) obtained at autopsy. Despite the homology with calcitonin gene-related peptide (CGRP), CGRP was a poor inhibitor of [125I]adrenomedullin binding (IC50 > 1 microM) compared with adrenomedullin(1-52) (IC50 = 1.2 +/- 0.5 nM, mean +/- SEM, n = 3). Three adrenomedullin fragments, adrenomedullin(1-12), adrenomedullin(22-52), and adrenomedullin(13-52), were also poor inhibitors of the binding (IC50 = 0.3 microM), suggesting that the whole molecule of adrenomedullin(1-52) is required for binding to the receptor. Scatchard plots of [125I]adrenomedullin binding in human brain (cerebral cortex) gave a dissociation constant of 0.17 +/- 0.03 nM and maximal binding of 99.3 +/- 1.9 fmol/mg protein (n = 5). These findings suggest that specific adrenomedullin binding sites that differ from the CGRP receptors exist in human brain. This indicates a possible novel neurotransmitter/neuromodulator role for adrenomedullin in human brain.

Pulmonary vasodilation to adrenomedullin: a novel peptide in humans

The present study investigates the effects of human adrenomedullin (ADM) on the pulmonary vascular bed of isolated, blood-perfused rat lung. Because pulmonary blood flow and left atrial pressure were constant, changes in pulmonary arterial pressure directly reflect changes in pulmonary vascular resistance. Under conditions of resting (low) pulmonary vasomotor tone, intra-arterial bolus injections of ADM-(1-52) and two truncated sequences of ADM-(1-52) [ADM-(1-12) and ADM-(13-52)] did not alter pulmonary arterial pressure. When pulmonary vasomotor tone was increased by U-46619, a thromboxane A2 mimic, intra-arterial bolus injections of ADM-(1-52) and ADM-(13-52) at similar doses produced similar, dose-dependent reductions in pulmonary arterial pressure. On a molar basis, ADM-(1-52) had greater pulmonary vasodilator activity than isoproterenol. In contrast, ADM-(1-12) had no activity. When pulmonary vasomotor tone was actively increased to the same level using KCl, the pulmonary vasodilator activity of ADM-(13-52) was decreased 10-fold. The present data demonstrate that ADM-(1-52) dilates the pulmonary vascular bed and suggest that the pulmonary vasodilator activity of ADM is greater on pulmonary blood vessels preconstricted through a receptor-dependent mechanism. Because meclofenamate, nitro-L-arginine methyl ester, methysergide, BW A-1433U83, U-37883A, and calcitonin gene-related peptide [CGRP-(8-37)], a CGRP-receptor antagonist, did not alter the pulmonary vasodilator response to ADM-(1-52), the present data suggest that ADM dilates the pulmonary vascular bed independently of cyclooxygenase products, endothelium-derived relaxation factor, serotoninergic receptors, adenosine1 purinoreceptors, ATP-dependent potassium channels, and CGRP receptors.(ABSTRACT TRUNCATED AT 250 WORDS)