Suc-Gly-Pro-Leu-Gly-Pro-AMC |
| Catalog No.GA23560 |
Suc-Gly-Pro-Leu-Gly-Pro-AMC, a highly sensitive, fluorogenic substrate for thimet oligopeptidase as well as for post-proline cleaving enzyme (prolyl endopeptidase).
Products are for research use only. Not for human use. We do not sell to patients.
Cas No.: 72698-36-3
Sample solution is provided at 25 µL, 10mM.
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Suc-Gly-Pro-Leu-Gly-Pro-AMC, a highly sensitive, fluorogenic substrate for thimet oligopeptidase as well as for post-proline cleaving enzyme (prolyl endopeptidase) [1].
The FAP activity in human plasma was measured using succinyl-pentapeptide composed of SUch-Gly-pro-Leu-Gly-pro-AMC, which contains two FAP cleavage sites.Only the cleavage between the last proline residue and the AMC group releases the fluorescent AMC group, resulting in a fluorescence reading, and the FAP activity of the measured samples ranges from 1.3 to 7 nM/min/ μL[2].
When each cell suspension was reacted with BODIPY FL casein and seven kinds of peptide-MCA substrates, respectively, a remarkable difference in hydrolytic activities toward Suc-GPLGP-MCA, a substrate toward collagenase-like peptidase, was observed between the constructs: Lc-Triad-displaying cells showed higher catalytic activity than Lc-WT-displaying cells[5].
In Male BALB/c mice ，using Suc-Gly-Pro-Leu-Gly-Pro-AMC test，no significant accumulations of other proteinases, such as matrix metalloproteinases, cathepsin D, and serine proteinases, were determined[3].Suc-GPLGP-MCA is hydro- lyzed at the Leu-Gly bond by CL-peptidase. The CL-peptidase activity in synovial fluid was significantly higher in patients with rheumatoid arthritis (RA) than in patients with osteoarthritis (OA) and in arthropathy-free controls[4].
References:
[1]: Kojima K, Kinoshita H, et,al. A new and highly sensitive fluorescence assay for collagenase-like peptidase activity. Anal Biochem. 1979 Nov 15;100(1):43-50. doi: 10.1016/0003-2697(79)90106-4. PMID: 232383.
[2]: Zhen EY, Jin Z, et,al. Circulating FGF21 proteolytic processing mediated by fibroblast activation protein. Biochem J. 2016 Mar 1;473(5):605-14. doi: 10.1042/BJ20151085. Epub 2015 Dec 3. PMID: 26635356; PMCID: PMC4764976.
[3]: Kakegawa H, Matano Y, et,al. Significant accumulations of cathepsin B and prolylendopeptidase in inflammatory focus of delayed-type hypersensitivity induced by Mycobacterium tuberculosis in mice. Biochem Biophys Res Commun. 2004 Mar 26;316(1):78-84. doi: 10.1016/j.bbrc.2004.01.176. PMID: 15003514.
[4]:Ito A, Hagihara M, et,al. Collagenase-like (CL) peptidase activity in synovial fluid from patients with rheumatoid arthritis. Clin Chim Acta. 1987 Dec;170(2-3):291-6. doi: 10.1016/0009-8981(87)90139-2. PMID: 2830060.
[5]:Okochi N, Kato-Murai M, et,al. Design of a serine protease-like catalytic triad on an antibody light chain displayed on the yeast cell surface. Appl Microbiol Biotechnol. 2007 Dec;77(3):597-603. doi: 10.1007/s00253-007-1197-0. Epub 2007 Sep 27. PMID: 17899065.
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