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A3832

Sigma-Aldrich

Adrenomedullin Fragment 22-52 human

≥97% (HPLC)

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About This Item

Empirical Formula (Hill Notation):
C159H252N46O48
CAS Number:
Molecular Weight:
3575.98
MDL number:
UNSPSC Code:
12352209
NACRES:
NA.26

product name

Adrenomedullin Fragment 22-52 human, ≥97% (HPLC)

Quality Level

Assay

≥97% (HPLC)

form

powder

color

white

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... ADM(133)

Amino Acid Sequence

Thr-Val-Gln-Lys-Leu-Ala-His-Gln-Ile-Tyr-Gln-Phe-Thr-Asp-Lys-Asp-Lys-Asp-Asn-Val-Ala-Pro-Arg-Ser-Lys-Ile-Ser-Pro-Gln-Gly-Tyr-NH2

Biochem/physiol Actions

Adrenomedullin Fragment 22-52 [ADM22-52] is used as an adrenomedullin (ADM) receptor antagonist to study the functions and mechanism of action of ADM signaling. ADM(22-52) is used to differentiate adrenomedullin binding sites in various cells and tissues.

Storage Class Code

11 - 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

Certificates of Analysis (COA)

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Agnieszka Ziolkowska et al.
International journal of molecular medicine, 11(5), 613-615 (2003-04-10)
Adrenomedullin (ADM) and its receptors are expressed in the adrenal cortex, where ADM is currently known to inhibit agonist-stimulated aldosterone secretion from zona glomerulosa (ZG), without affecting either basal aldosterone release or the secretory activity of zona fasciculata-reticularis (ZF/R) cells.
Jing Hui Yang et al.
Regulatory peptides, 158(1-3), 19-25 (2009-06-16)
Intermedin (IMD) is a novel peptide related to calcitonin gene-related peptide (CGRP) and adrenomedullin (ADM). Proteolytic processing of a larger precursor of IMD yields a biologically active C-terminal fragment IMD(1-53). We aimed to observe the cardioprotective antifibrotic effects of IMD(1-53)
Christian Juaneda et al.
European journal of pharmacology, 474(2-3), 165-174 (2003-08-19)
The existence of specific adrenomedullin receptor binding sites was investigated using the agonist peptide fragment [125I]human adrenomedullin-(13-52) in rat brain, lung and vas deferens homogenates. Saturation-binding experiments suggest that [125I]human adrenomedullin-(13-52) binds to an apparent single population of sites with
Takahisa Ishikawa et al.
Oncogene, 22(8), 1238-1242 (2003-02-28)
Since it is reported that adrenomedullin (AM) upregulated by hypoxia inhibits hypoxic cell death, we examined the effects of AM antagonist (AM C-terminal fragment; AM(22-52)) on the growth of pancreatic cancer cells. We, for the first time, demonstrated that AM
Benjamin Uzan et al.
Journal of cellular physiology, 215(1), 122-128 (2007-10-18)
Adrenomedullin (ADM) has been shown to mediate multifunctional responses in cell culture and animal system such as regulation of growth and apoptosis. ADM stimulates the proliferation of osteoblasts in vitro and promotes bone growth in vivo. The ability of ADM

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