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Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Additionally we are shipping MMP12 Kits (60) and MMP12 Proteins (34) and many more products for this protein.
Showing 10 out of 194 products:
Human Polyclonal MMP12 Primary Antibody for EIA, IHC (p) - ABIN358685
Nar, Werle, Bauer, Dollinger, Jung: Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor. in Journal of molecular biology 2001
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Human Polyclonal MMP12 Primary Antibody for IF, IHC (p) - ABIN390136
Shapiro, Kobayashi, Ley: Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages. in The Journal of biological chemistry 1993
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Human Polyclonal MMP12 Primary Antibody for WB - ABIN223237
Ikonomidis, Jones, Barbour, Stroud, Clark, Kaplan, Zeeshan, Bavaria, Gorman, Spinale, Gorman: Expression of matrix metalloproteinases and endogenous inhibitors within ascending aortic aneurysms of patients with bicuspid or tricuspid aortic valves. in The Journal of thoracic and cardiovascular surgery 2007
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Human Polyclonal MMP12 Primary Antibody for ELISA, WB - ABIN4334937
Mirowska-Guzel, Gromadzka, Czlonkowski, Czlonkowska: Association of MMP1, MMP3, MMP9, and MMP12 polymorphisms with risk and clinical course of multiple sclerosis in a Polish population. in Journal of neuroimmunology 2009
Mmp12 is expressed early following corneal epithelial injury with highest expression levels at 8 h after injury and lower expression levels at 4 and 8 days after injury. We investigated whether MMP12 has an effect on the rate of epithelial repair and cell migration using in vivo and in vitro scratch assays performed on WT and Mmp12(-/-) mice
MMP-12 produced by macrophages infiltrating into glomeruli contributed to the degradation of collagen type IV (show COL4 Antibodies) and fibronectin (show FN1 Antibodies).
MMP12 causes arterial stiffening in mice and suggest that it functions similarly in humans.
These results suggest that MMP-12 production during emphysema exacerbation results in increased mortality and disease progression.
study found significant increases of MMP-3 (show MMP3 Antibodies) and MMP-12 mRNA levels and MMP12 zymographic activities in response to Cryptococcus neoformans infection but not C. gattii infection
The results suggest that pulmonary C fiber involvement in long-term airway inflammation and airway hyperresponsiveness occurred at least partially via modulating MMP-12, and the activation of PAR2 (show F2RL1 Antibodies) might be related to MMP-12 production.
MMP-12 up-regulation mediated by SARM (show SARM1 Antibodies)-TRIF (show RNF138 Antibodies) signaling pathway contributes to IFN-gamma (show IFNG Antibodies)-independent airway inflammation and AHR (show AHR Antibodies) post RSV infection in nude mice.
MMP-12 and MMP-13 (show MMP13 Antibodies) alter strain K infection in mice and play a role in inflammatory regulation by modulating cytokine levels.
Post-MI, MMP-12i impaired CD44 (show CD44 Antibodies)-HA interactions to suppress neutrophil apoptosis and prolong inflammation, which worsened LV function.
MMP12 upregulated in regenerating motor neurons of the mouse and rat facial nucleus; findings point to a role of MMP12 in the neuronal initiation of the synaptic stripping process
Data indicate that MMP1 (show MMP1 Antibodies), MMP12 and PPARG (show PPARG Antibodies) and hsa (show CD24 Antibodies)-miR (show MLXIP Antibodies)-31-5p, hsa (show CD24 Antibodies)-miR (show MLXIP Antibodies)-224-5p, and hsa (show CD24 Antibodies)-miR (show MLXIP Antibodies)-223-3p were able to distinguish tumors from NPT with high sensitivity and specificity.
Increased levels of MMP1 (show MMP1 Antibodies) and MMP12 on tumor-associated macrophages in the peripheral areas of dermatofibrosarcoma protuberance might contribute to local invasion
Matrix metalloprotease (show ADAM8 Antibodies) (MMP) regulation was the top pathway involved in gingival aging. MMP3 (show MMP3 Antibodies), MMP9 (show MMP9 Antibodies), MMP12, and MMP13 (show MMP13 Antibodies) were upregulated in old gingival tissues, concomitantly with interleukin-1 beta (IL1B (show IL1B Antibodies)) expression.
We also found that MMP12 facilitated type I collagen induced platelet aggregation, adhesion and alpha granule secretion. Similarly, one short peptide, WYKG, facilitated type I collagen induced platelet alpha granule secretion. We conclude that platelet express MMP12 may facilitate platelet activation through shedding of CEACAM1 (show CEACAM1 Antibodies).
There were no statistically significant differences in the distribution of MMP7 (show MMP7 Antibodies) -181 A/G and MMP12 -82 A/G genotype, allele, or haplotype frequencies between IRSA patients and controls, as well as patients' primary and secondary idiopathic recurrent spontaneous abortion
To conclude, Pseudomonas aeruginosa infection induced the expression of matrix metalloproteinases, and Pseudomonas aeruginosa type III secretion system appeared to be a key player in MMP-12 and MMP-13 (show MMP13 Antibodies) expression, which is further controlled by NF-kappaB (show NFKB1 Antibodies) signaling.
This study demonstrated that the MMP-12 levels was significantly higher in patients with atheromatous plaques than in those without plaques.
High MMP12 expression is associated with gastric cancer.
Study evaluated MMP-12 and TIMP-1 (show TIMP1 Antibodies), TIMP-2 (show TIMP2 Antibodies), TIMP-3 (show TIMP3 Antibodies), and TIMP-4 (show TIMP4 Antibodies) levels in 40 patients with asymptomatic and symptomatic critical carotid artery stenosis (CAS (show CSE1L Antibodies)) with neurologic symptoms onset within the preceding 12 hours; results suggest that MMP-12 is related to critical CAS (show CSE1L Antibodies) independently on symptoms, moreover, TIMP-3 (show TIMP3 Antibodies) and TIMP-4 (show TIMP4 Antibodies) seem to be specifically related to stroke
Gene expression profiling performed on tissues obtained from pulmonary sarcoidosis patients identified MMP12 as a potential pathogenic mediator of lung damage and/or remodeling and may serve as a marker for this disease.
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. It is thought that the protein encoded by this gene is cleaved at both ends to yield the active enzyme, but this processing has not been fully described. The enzyme degrades soluble and insoluble elastin. It may play a role in aneurysm formation and studies in mice suggest a role in the development of emphysema. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
matrix metallopeptidase 12 (macrophage elastase)
, matrix metalloproteinase 12
, macrophage elastase
, macrophage metalloelastase
, matrix metalloproteinase-12
, matrix metalloproteinase 12 (macrophage elastase)
, macrophage metalloelastase MMP-12