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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 (79) and MMP8 Proteins (24) and many more products for this protein.
Showing 10 out of 158 products:
Human Polyclonal MMP8 Primary Antibody for EIA, IHC (p) - ABIN358702
Van den Steen, Husson, Proost, Van Damme, Opdenakker: Carboxyterminal cleavage of the chemokines MIG and IP-10 by gelatinase B and neutrophil collagenase. in Biochemical and biophysical research communications 2003
Show all 4 references for ABIN358702
Human Monoclonal MMP8 Primary Antibody for FACS, IHC - 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 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
Human Polyclonal MMP8 Primary Antibody for IHC (p), WB - ABIN390153
Massova, Kotra, Fridman, Mobashery: Matrix metalloproteinases: structures, evolution, and diversification. in FASEB journal : official publication of the Federation of American Societies for Experimental Biology 1998
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
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.
Suggest that MMP8 plays an important role in angiogenesis in vitro and in vivo.
MMP8 plays an important role in stem cell migration and their recruitment into atherosclerotic lesions.
infiltrative pulmonary tuberculosis is characterized by impairements in the system MMP/inhibitors: the levels of MMP-1 (show MMP1 Antibodies), -9 increased, MMP-3 (show MMP3 Antibodies), -8, TIMP-1 (show TIMP1 Antibodies) remained at the reference values and a 2-macroglobulin was low.
Serum level patterns of MMP-2 (show MMP2 Antibodies) and MMP-8 showed distinctive patterns for patients with spinal cord injury neurological impairment. MMP-8 and MMP-9 (show MMP9 Antibodies) patterns showed significant differences regarding functional recovery. Our binary logistic regression model showed that, according to neurological damage, measuring peripheral serum levels can be used to monitor and predict locomotor recovery after spinal cord injury.
Blood expression of matrix metalloproteinases 8 and 9 and of their inducers S100A8 (show S100A8 Antibodies) and S100A9 (show S100A9 Antibodies) supports diagnosis and prognosis of PDAC-associated diabetes mellitus
Plasma MMP-8 and MMP-9 (show MMP9 Antibodies) concentrations correlate with diabetic ketoacidosis severity and are known to degrade brain microvascular endothelial cell tight junctions. Thus, leukocyte-derived MMPs might contribute to DKA-associated cerebrovascular complications.
Initial analysis of the MMP8 gene showed suggestive association between rs1940475 and knee OA, but the finding did not replicate in other study cohorts, even though the trend for predisposing allele was similar in all five cohorts. MMP-8 is a good biological candidate for OA, but our study did not find common variants with significant association in the gene.
Sputum, serum, and urine MMP-8 were not significantly changed in COPD (show ARCN1 Antibodies) exacerbation compared to recovery values.
EMMPRIN, MMP8, hyaluronan, beta-defensing-2, and neutrophil gelatinase-associated lipocalin (NGAL (show LCN2 Antibodies)) are elevated in women with vaginal inflammation
Suggest that MMP-8 polymorphism -799 C/T was a risk for developing chronic periapical lesions.
The reciprocal positive interplay between MMP-8 and TGF-beta1 contributes to HCC invasion and metastasis by inducing EMT mainly through the PI3K/Akt/Rac1 pathway.
increased levels in saliva (show RAG1AP1 Antibodies) and serum in women with polycystic ovary syndrome, and is potentiated in the presence of gingivitis
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)