Angiotensin II, human, ClearPoint™ Ile labeled (13C and 15N) - 0.1 mg
- Cat.Number : AS-64805
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This peptide is angiontensin II (Ang II) with Isoleucine universally labeled with 13C and 15N. The octapeptide angiotensin II (Ang II) exerts a wide range of effects on the cardiovascular system. It is also implicated in the regulation of cell proliferation, fibrosis and apoptosis. Ang II is formed through cleavage of Ang I by the angiotensin-converting enzyme (ACE) or chymases. Human heart chymase, a chymotrypsin-like serine proteinase, hydrolyzes the Phe8-His9 bond to yield the octapeptide hormone angiotensin II and His-Leu.
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            References
Angiotensin converting enzyme-like activity in tissues from the river lamprey or lampern, Lampetra fluviatilis, acclimated to freshwater and seawater
Gen Comp Endocrinol . 2002 Jun 01 ; 127 (1) | DOI : https://doi.org/10.1016/S0016-6480(02)00014-X
- C Cobb,
Cooperation between Mast Cell Carboxypeptidase A and the Chymase Mouse Mast Cell Protease 4 in the Formation and Degradation of Angiotensin II
JBC . 2004 Jun 01 ; 279 32339 | DOI : 10.1074/jbc.M405576200
- A. Lundequist
Comparison of the solution structures of angiotensin I & II: Implication for structure-function relationship
Eur J Biochem . 2003 Apr 22 ; 270 2163 | DOI : https://doi.org/10.1046/j.1432-1033.2003.03573.x
- G. Spyroulias
Multiple determinants for the high substrate specificity of an angiotensin II-forming chymase from the human heart.
JBC . 1991 Oct 15 ; 266 19192
- A. Kinoshita
Angiotensin converting enzyme-like activity in tissues from the river lamprey or lampern, Lampetra fluviatilis, acclimated to freshwater and seawater
Gen Comp Endocrinol . 2002 Jun 01 ; 127(1) 8 | DOI : https://doi.org/10.1016/S0016-6480(02)00014-X
- C Cobb,
- et al
Cooperation between Mast Cell Carboxypeptidase A and the Chymase Mouse Mast Cell Protease 4 in the Formation and Degradation of Angiotensin I
J Biol Chem . 2004 Jul 01 ; 279(31) 32339 | DOI : https://doi.org/10.1074/jbc.M405576200
- A. Lundequist
- et al
Multiple determinants for the high substrate specificity of an angiotensin II-forming chymase from the human heart.
J Biol Chem . 1991 Oct 01 ; 266(29) 19192 | DOI : https://doi.org/10.1016/S0021-9258(18)54981-4
- A. Kinoshita
- et al
