M9695
Matrix Metalloproteinase-12, Catalytic Domain human
recombinant, expressed in E. coli, ≥95% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
MMP-12, Macrophage Elastase
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About This Item
Recommended Products
recombinant
expressed in E. coli
Quality Level
Assay
≥95% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
calculated mol wt 20.3 kDa
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... MMP12(4321)
General description
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 Actions
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.
Unit Definition
One unit equals 100 pmol/min at 37 °C using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt as substrate.
Physical 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.
Legal Information
Brij is a registered trademark of Croda International PLC
Hazard Statements
Precautionary Statements
Hazard Classifications
Aquatic Chronic 3
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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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