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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 MMP8 Kits (106) and MMP8 Proteins (23) and many more products for this protein.
Showing 10 out of 183 products:
Human Polyclonal MMP8 Primary Antibody for IF (p), IHC (p) - ABIN736283
Zhang, Li, Zhang, Fu, Cui: Hydrogen sulfide suppresses the expression of MMP-8, MMP-13, and TIMP-1 in left ventricles of rats with cardiac volume overload. in Acta pharmacologica Sinica 2013
Show all 2 Pubmed References
Human Monoclonal MMP8 Primary Antibody for CyTOF, FACS - ABIN4899598
Arechavaleta-Velasco, Marciano, Díaz-Cueto, Parry: Matrix metalloproteinase-8 is expressed in human chorion during labor. in American journal of obstetrics and gynecology 2004
Human Polyclonal MMP8 Primary Antibody for IHC, IHC (p) - ABIN4335077
Ong, Elkington, Brilha, Ugarte-Gil, Tome-Esteban, Tezera, Pabisiak, Moores, Sathyamoorthy, Patel, Gilman, Porter, Friedland: Neutrophil-Derived MMP-8 Drives AMPK-Dependent Matrix Destruction in Human Pulmonary Tuberculosis. in PLoS pathogens 2015
Human Polyclonal MMP8 Primary Antibody for IP, IHC - ABIN223233
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
MMP8 plays an important role in intestinal I/R injury through mechanisms involving increased inflammation and loss of claudin-3 (show CLDN3 Antibodies)
These results suggest that some of the anti-inflammatory effects of Dexamethasone are mediated through increased MMP-8 expression.
These results suggest a novel pathogenetic role of MMP8 and implicate modulation of its activity as a tractable strategy for therapies against cerebral ischemia.
Fusion peptide inhibitors of MMP-8/-9 prevent endotoxic shock if administered within a strict time window.
the loss of MMP-8 likely has pleiotropic effects on innate immunity and angiogenesis that are reflected in changes in the protease web.
A previously unknown role of MMP8 in M2-macrophage polarization by cleaving fibromodulin (show FMOD Antibodies) and therefore increasing the bioavailability of TGF-beta (show TGFB1 Antibodies).
MMP-8-deficient mice had significantly lower serum triglyceride (TG) levels (P = 0.003) and larger HDL (show HSD11B1 Antibodies) particles compared with wild-type (WT) mice. However, no differences were observed in the apoA-I (show APOA1 Antibodies) levels.
These results demonstrate that MMP-8 critically mediates microglial activation by modulating TNF-alpha (show TNF Antibodies) activity, which may explain neuroinflammation in septic mouse brain.
MMP-13 (show MMP13 Antibodies) prevails over MMP-8 in collagen degradation in atheromata.
MMP8 enhances vascular smooth muscle cell proliferation via an ADAM10 (show ADAM10 Antibodies), N-cadherin (show CDH2 Antibodies), and beta-catenin (show CTNNB1 Antibodies)-mediated pathway and plays an important role in neointima formation.
Data show that individuals with MMP-8 -799TT genotype and intermediate HIV disease stage are at higher risk for the advancement of HIV disease. MMP-8 polymorphism indicated a trend of elevated risk for the modulation of HIV-associated neurocognitive disorder (HAND) severity. MMP-8 -799TT genotype may facilitate the risk for the development of HAND with tobacco and alcohol usage.
The serum levels of IL-8 (show IL8 Antibodies), MIP-1 alpha (show CCL3 Antibodies), MIP-1 beta (show CCL4 Antibodies), MMP-8, Resistin (show RETN Antibodies), FLRG (show FSTL3 Antibodies), and BCAM (show BCAT2 Antibodies) were significantly higher in breast cancer patients, but LAP and TSH-beta (show TSHB Antibodies) levels were lower.
Matrix metalloproteinase-1 (show MMP1 Antibodies), -8, -9 and the risk of cardiovascular complications in patients with CHD (show CHDH Antibodies) before and after myocardial revascularization.
Our study provides evidence for the tumour-suppressive mechanisms of MMP-8 in OTSCC by interplay with TGF-b1 and VEGF-C (show VEGFC Antibodies).
These results provide the first evidence that MMP8 SNP at the rs11225394 locus is associated with the increased risk of osteonecrosis of the femoral head in Chinese Han population.
Low MMP-8/TIMP-1 (show TIMP1 Antibodies) reflects left ventricle impairment in takotsubo cardiomyopathy and high TIMP-1 (show TIMP1 Antibodies) may help to differentiate it from acute coronary syndrome
Plasma levels of MMP-1 (show MMP1 Antibodies), MMP-8, and MMP-9 (show MMP9 Antibodies) are associated with COPD (show ARCN1 Antibodies) severity and can be used as a biomarker to better understand the characteristics of COPD (show ARCN1 Antibodies) patients.
there is a negative correlation between blood MMP8 and HDL (show HSD11B1 Antibodies)-cholesterol levels, suggesting a contributory role of MMP8 in metabolic alterations in acne inversa
plasma concentrations of MMP-7 (show MMP7 Antibodies), MMP-8, -9 and TIMP-1 (show TIMP1 Antibodies) within 96 h from the onset of acute pancreatitis symptoms are elevated in acute pancreatitis patients compared with healthy controls
MMP-8 is a vital component of the myoepithelial tumour-suppressor function. It restores MEC (show CCL28 Antibodies) interaction with the matrix, opposes TGF-beta (show TGFB1 Antibodies) signalling and MMP-9 (show MMP9 Antibodies) proteolysis, which contributes to inhibition of tumour cell invasion.
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. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage. Its function is degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
matrix metallopeptidase 8 (neutrophil collagenase)
, matrix metalloproteinase 8
, collagenase 2
, matrix metalloproteinase-8
, neutrophil collagenase
, neutrophil collagenease
, PMNL collagenase
, matrix metalloproteinase 8 (neutrophil collagenase)