product name
MMP Substrate,
检测方案
≥95% (HPLC)
形式
lyophilized
组成
Peptide Content, ≥75%
储存条件
protect from light
储存温度
−20°C
Amino Acid Sequence
MCA-Lys-Pro-Leu-Gly-Leu-DNP-Dpa-Ala-Arg-NH2
一般描述
Matrix Metalloproteases (MMPs) belongs to the zinc metalloprotease family M10. They are zinc-dependent, calcium-containing hydrolases.
生化/生理作用
Matrix Metalloproteases (MMPs) are involved in extracellular matrix (ECM) degradation. MMPs regulate cellular and disease processes. They are implicated in processes such as cell proliferation, migration, differentiation, angiogenesis, anti-inflammatory response, vasoconstriction, apoptosis and host defense. Dysregulation of MMP is associated with arthritis, ulcers, encephalomyelitis and cancer.
The peptide MCA-Lys-Pro-Leu-Gly-Leu-DNP-Dpa-Ala-Arg-NH2, or FS-6, is a fluorogenic substrate for several matrix metalloproteinases (MMPs). FS-6 is a water-soluble, modified form of the well-established MMP substrate FS-1, where a lysine residue has been added to the N-terminus of FS-1. The resulting FS-6 has been reported to give a peptide with improved kinetic properties for several MMPs, including MMP-1, MMP-8, MMP-13, and MMP-14, compared to FS-1. This MMP substrate has also been described as a particularly useful substrate for the zinc metalloproteinase tumor necrosis factor-α converting enzyme (TACE or ADAM-17). FS-6 can be used to measure metalloproteinase activity in tissue culture conditions, for example, on the surface of viable cells in situ.
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
常规特殊物品
Knowledge-transfer learning for prediction of matrix metalloprotease substrate-cleavage sites
Wang Y, et al.
Scientific Reports, 7(1), 5755-5755 (2017)
Ulf Neumann et al.
Analytical biochemistry, 328(2), 166-173 (2004-04-29)
Matrix metalloproteinases (MMPs) and the related tumor necrosis factor converting enzyme (TACE) are involved in tissue remodeling, cell migration, and processing of signaling molecules, such as cytokines and adhesion molecules. Fluorescence-quenched peptide substrates have been widely used to quantitate the
MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity.
Bhaskaran R
The Journal of Biological Chemistry, 283(31), 21779-21788 (2008)
Hideaki Nagase et al.
Cardiovascular research, 69(3), 562-573 (2006-01-13)
Matrix metalloproteinases (MMPs), also called matrixins, function in the extracellular environment of cells and degrade both matrix and non-matrix proteins. They play central roles in morphogenesis, wound healing, tissue repair and remodelling in response to injury, e.g. after myocardial infarction
David J Wilkinson et al.
The FEBS journal (2021-07-17)
Matrix metalloproteinase-13 (MMP-13) is a uniquely important collagenase that promotes the irreversible destruction of cartilage collagen in osteoarthritis (OA). Collagenase activation is a key control point for cartilage breakdown to occur, yet our understanding of the proteinases involved in this
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