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SCP0192

Sigma-Aldrich

MMP 2 Substrate, fluorogenic

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Empirical Formula (Hill Notation):
C49H68N14O15
Molecular Weight:
1093.15
NACRES:
NA.32

assay

≥95% (HPLC)

form

lyophilized

composition

Peptide Content, ≥73%

storage condition

protect from light

storage temp.

−20°C

Amino Acid Sequence

MCA-Pro-Leu-Ala-Nva-DNP-Dap-Ala-Arg-NH2

General description

Matrix metalloproteinases (MMPs) are localized to the nucleus, mitochondria, vesicles and cytoplasm. MMP family comprises of 25 members, of which 24 are present in mammals. MMPs are encoded as inactive enzymes and are localized to cell membranes. All MMP members possess pro domain (80 amino acids) and catalytic domains.

Application

Matrix metalloproteinases (MMP) are a family of zinc-dependent endopeptidases that degrade matrix proteins. MMPs include collagenases, gelatinases, matrilysins, enamelysins, metalloelastases, stromelysins and other structural protein and receptor lysins. The activity of these enzymes is selectively inhibited or measured by appropriately labeled peptides. MCA-Pro-Leu-Ala-Nva-DNP-Dap-Ala-Arg-NH2; DNP-Pro-Leu-Gly-Met-Trp-Ser-Arg (DNP-PLGMWSR), Dnp-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2 (DNP-PLGLWA-D-R-NH2), Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH (DNP-PQGIAGQ-D-R-OH) and MOCAc [(7-methoxy coumarin-4-yl) acetyl]-RPKPYANvaWMK(Dnp[2,4-dinitrophenyl])-NH(2) are substrates for matrix metalloproteinase 2.

Biochem/physiol Actions

Matrix metalloproteinases (MMPs) are responsible for degrading membrane proteins, such as basal lamina proteins of cerebral blood vessels. Proteolysis of intracellular substrates by MMPs is associated with the innate immune system and apoptosis. They are also involved in disease conditions such as oncogenesis, cardiac, neurological and autoimmune disorders. MMPs are also associated with pathogenesis related to protein conformational changes. Elevated expression of a number of MMPs is observed in myocardial infarction and heart failure.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Matrix Metalloproteinases In Health And Disease: Sculpting The Human Body (2017)
Control of matrix metalloproteinase catalytic activity
Ra HJ and Parks WC
Matrix Biology, 26(8), 587-596 (2007)
Matrix Metalloproteinase Biology, 11-11 (2015)
Maria Orfanoudaki et al.
Marine drugs, 18(1) (2020-01-08)
Mycosporine-like amino acids (MAAs) are water-soluble metabolites, reported to exhibit strong UV-absorbing properties. They have been found in a wide range of marine organisms, especially those that are exposed to extreme levels of sunlight, to protect them against solar radiation.
Matrix metalloproteinase-mediated disruption of tight junction proteins in cerebral vessels is reversed by synthetic matrix metalloproteinase inhibitor in focal ischemia in rat
Yang YI
Journal of Cerebral Blood Flow and Metabolism, 27(4), 697-709 (2007)

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