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Human ADM / Adrenomedullin Protein (Fc Tag)

AM,PAMP

Catalog Number P11646-H01H
Organism Species Human
Host Human Cells
Synonyms AM,PAMP
Molecular Weight The recombinant human ADM/Fc is a disulfide-linked homodimer. The reduced monomer comprises 340 amino acids and has a predicted molecular mass of 38 kDa. The apparent molecular mass of the protein is approximately 39 in SDS-PAGE under reducing conditions due to glycosylation.
predicted N Glu
SDS-PAGE
Purity > 93 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human ADM (P35318) (Tyr95-Tyr146) was expressed, with the fused Fc region of human IgG1 at the N-terminus.
Bio-activity
Research Area Cancer |Invasion microenvironment |Angiogenesis |Growth Factor & Receptor |Hormones
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Adrenomedullin consists of 52 amino acids and is a member of the adrenomedullin family. It s a a hypotensive peptide and has 1 intramolecular disulfide bond. It seems that adrenomedullin has a slight homology with the calcitonin gene-related peptide. Adrenomedullin has a highly expression in pheochromocytoma and adrenal medulla. It also can be detected in lung, ventricle and kidney tissues. Adrenomedullin and PAMP are potent hypotensive and vasodilatator agents. Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, adrenomedullin is diuretic and natriuretic, and both adrenomedullin and PAMP inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels. It is believed that adrenomedullin functions through combinations of the calcitonin receptor like receptor and receptor activity-modifying proteins complexes, as well as CGRP receptors.
Reference
  • Hao SL, et al. (2011) The antifibrosis effect of adrenomedullin in human lung fibroblasts. Exp Lung Res. 37(10):615-26.
  • Hikosaka T, et al. (2011) Adrenomedullin production is increased in colorectal adenocarcinomas; its relation to matrix metalloproteinase-9. Peptides. 32(9):1825-31.
  • Boc-Zalewska A, et al. (2011) Adrenomedullin mRNA expression in placenta of preeclamptic women. Ginekol Pol. 82(8):585-91.
  • Palladini G, et al. (2011) Midregional proadrenomedullin (MR-proADM) is a powerful predictor of early death in AL amyloidosis. Amyloid. 18(4):216-21.