M9695
Matrix Metalloproteinase-12, Catalytic Domain human
recombinant, expressed in E. coli, ≥95% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(e):
MMP-12, Macrophage Elastase
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About This Item
Empfohlene Produkte
Rekombinant
expressed in E. coli
Qualitätsniveau
Assay
≥95% (SDS-PAGE)
Form
buffered aqueous glycerol solution
Mol-Gew.
calculated mol wt 20.3 kDa
UniProt-Hinterlegungsnummer
Versandbedingung
dry ice
Lagertemp.
−70°C
Angaben zum Gen
human ... MMP12(4321)
Allgemeine Beschreibung
Matrix metalloproteinase-12 (MMP-12) is also called as macrophage metalloelastase and is secreted by inflammatory macrophages. It is synthesized as a zymogen and then activated by cleaving the propeptide domain. The MMP-12 gene is localized on chromosome 11.
Biochem./physiol. Wirkung
MMP-12 degrades general matrix components and may have a role in processes such as host defense, cell proliferation, and protein turnover as well as tissue remodeling.
Matrix metalloproteinase-12 (MMP-12) breaks down proteoglycans, collagen type IV and laminin. Its main substrate is elastin.
Einheitendefinition
One unit equals 100 pmol/min at 37 °C using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt as substrate.
Physikalische Form
Solution in 50 mM Tris, 5 mM calcium chloride, 500 mM sodium chloride, 20 μM zinc chloride, 0.5% Brij® L23, and 30% glycerol, pH 9.5.
Rechtliche Hinweise
Brij is a registered trademark of Croda International PLC
H-Sätze
P-Sätze
Gefahreneinstufungen
Aquatic Chronic 3
Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 2
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Gloves, multi-purpose combination respirator cartridge (US)
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S D Shapiro
Current opinion in cell biology, 10(5), 602-608 (1998-11-18)
Targeted mutagenesis has allowed investigators to perform controlled experiments in mammals and determine the contribution of individual proteins to physiologic and pathologic processes. Recent lessons learned from matrix metalloproteinase gene targeted mice and other in vivo observations have given new
S D Shapiro et al.
The Journal of biological chemistry, 268(32), 23824-23829 (1993-11-15)
Human alveolar macrophages have the capacity to degrade elastin. As an approach to define proteinases responsible for this activity, we recently cloned a murine macrophage elastase cDNA and demonstrated that it is a member of the matrix metalloproteinase gene family
Matthew Traylor et al.
PLoS genetics, 10(7), e1004469-e1004469 (2014-08-01)
Genome-wide association studies (GWAS) have begun to identify the common genetic component to ischaemic stroke (IS). However, IS has considerable phenotypic heterogeneity. Where clinical covariates explain a large fraction of disease risk, covariate informed designs can increase power to detect
Yi Song et al.
BMC cardiovascular disorders, 13, 34-34 (2013-05-07)
Aortic dissection(AD) is an acute process of large blood vessels characterized by dangerous pathogenic conditions and high disability and high mortality. The pathogenesis of AD remains debated. Matrix metalloproteinase-12 (MMP-12) participates in many pathological processes such as abdominal aortic aneurysm
A Belaaouaj et al.
The Journal of biological chemistry, 270(24), 14568-14575 (1995-06-16)
Human macrophage metalloelastase (HME) is a recent addition to the matrix metalloproteinase (MMP) family that was initially found to be expressed in alveolar macrophages of cigarette smokers. To understand more about HME expression, analysis of the structure and location of
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