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Merck
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主要文件

SCP0193

Sigma-Aldrich

MMP Substrate

≥95% (HPLC), lyophilized

别名:

FS-6

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About This Item

经验公式(希尔记法):
C55H80N16O16
分子量:
1221.32
分類程式碼代碼:
12352200
NACRES:
NA.32

product name

MMP Substrate,

化驗

≥95% (HPLC)

形狀

lyophilized

成份

Peptide Content, ≥75%

儲存條件

protect from light

儲存溫度

−20°C

Amino Acid Sequence

MCA-Lys-Pro-Leu-Gly-Leu-DNP-Dpa-Ala-Arg-NH2

一般說明

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.

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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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)
Knowledge-transfer learning for prediction of matrix metalloprotease substrate-cleavage sites
Wang Y, et al.
Scientific Reports, 7(1), 5755-5755 (2017)
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

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