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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. Zusätzlich bieten wir Ihnen MMP8 Kits (103) und MMP8 Proteine (23) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 182 products:
Human Polyclonal MMP8 Primary Antibody für 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 Polyclonal MMP8 Primary Antibody für 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
Human Polyclonal MMP8 Primary Antibody für 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 Monoclonal MMP8 Primary Antibody für 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
MMP8 plays an important role in intestinal I/R injury through mechanisms involving increased inflammation and loss of claudin-3 (zeige CLDN3 Antikörper)
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 (zeige FMOD Antikörper) and therefore increasing the bioavailability of TGF-beta (zeige TGFB1 Antikörper).
MMP-8-deficient mice had significantly lower serum triglyceride (TG) levels (P = 0.003) and larger HDL (zeige HSD11B1 Antikörper) particles compared with wild-type (WT) mice. However, no differences were observed in the apoA-I (zeige APOA1 Antikörper) levels.
These results demonstrate that MMP-8 critically mediates microglial activation by modulating TNF-alpha (zeige TNF Antikörper) activity, which may explain neuroinflammation in septic mouse brain.
MMP-13 (zeige MMP13 Antikörper) prevails over MMP-8 in collagen degradation in atheromata.
MMP8 enhances vascular smooth muscle cell proliferation via an ADAM10 (zeige ADAM10 Antikörper), N-cadherin (zeige CDH2 Antikörper), and beta-catenin (zeige CTNNB1 Antikörper)-mediated pathway and plays an important role in neointima formation.
The serum levels of IL-8 (zeige IL8 Antikörper), MIP-1 alpha (zeige CCL3 Antikörper), MIP-1 beta (zeige CCL4 Antikörper), MMP-8, Resistin (zeige RETN Antikörper), FLRG (zeige FSTL3 Antikörper), and BCAM (zeige BCAT2 Antikörper) were significantly higher in breast cancer patients, but LAP and TSH-beta (zeige TSHB Antikörper) levels were lower.
Matrix metalloproteinase-1 (zeige MMP1 Antikörper), -8, -9 and the risk of cardiovascular complications in patients with CHD (zeige CHDH Antikörper) 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 (zeige VEGFC Antikörper).
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 (zeige TIMP1 Antikörper) reflects left ventricle impairment in takotsubo cardiomyopathy and high TIMP-1 (zeige TIMP1 Antikörper) may help to differentiate it from acute coronary syndrome
Plasma levels of MMP-1 (zeige MMP1 Antikörper), MMP-8, and MMP-9 (zeige MMP9 Antikörper) are associated with COPD (zeige ARCN1 Antikörper) severity and can be used as a biomarker to better understand the characteristics of COPD (zeige ARCN1 Antikörper) patients.
there is a negative correlation between blood MMP8 and HDL (zeige HSD11B1 Antikörper)-cholesterol levels, suggesting a contributory role of MMP8 in metabolic alterations in acne inversa
plasma concentrations of MMP-7 (zeige MMP7 Antikörper), MMP-8, -9 and TIMP-1 (zeige TIMP1 Antikörper) 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 (zeige CCL28 Antikörper) interaction with the matrix, opposes TGF-beta (zeige TGFB1 Antikörper) signalling and MMP-9 (zeige MMP9 Antikörper) proteolysis, which contributes to inhibition of tumour cell invasion.
a 7-gene signature was identified which correctly predicted the primary prefibrotic myelofibrosis group with a sensitivity of 100% and a specificity of 89%. The 7 genes included MPO (zeige MPO Antikörper), CEACAM8, CRISP3 (zeige CRISP3 Antikörper), MS4A3 (zeige MS4A3 Antikörper), CEACAM6, HEMGN, and MMP8
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)