SCP0192
MMP 2 Substrate, fluorogenic
≥95% (HPLC), lyophilized
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About This Item
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product name
MMP 2 Substrate, fluorogenic,
Ensaio
≥95% (HPLC)
forma
lyophilized
composição
Peptide Content, ≥73%
condição de armazenamento
protect from light
temperatura de armazenamento
−20°C
Amino Acid Sequence
MCA-Pro-Leu-Ala-Nva-DNP-Dap-Ala-Arg-NH2
Descrição geral
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.
Aplicação
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.
Ações bioquímicas/fisiológicas
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.
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Certificados de análise (COA)
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Control of matrix metalloproteinase catalytic activity
Matrix Biology, 26(8), 587-596 (2007)
Matrix metalloproteinase-mediated disruption of tight junction proteins in cerebral vessels is reversed by synthetic matrix metalloproteinase inhibitor in focal ischemia in rat
Journal of Cerebral Blood Flow and Metabolism, 27(4), 697-709 (2007)
Matrix Metalloproteinases In Health And Disease: Sculpting The Human Body (2017)
Matrix Metalloproteinase Biology, 11-11 (2015)
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.
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