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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 Antibodies (143) and MMP8 Kits (86) and many more products for this protein.
Showing 10 out of 26 products:
Human MMP8 Protein expressed in HEK-293 - ABIN2666511
Fang, Wen, Zhang, Lin, Moore, Wu, Ye, Xiao: An important role of matrix metalloproteinase-8 in angiogenesis in vitro and in vivo. in Cardiovascular research 2013
Show all 6 references for ABIN2666511
Human MMP8 Protein expressed in Human Cells - ABIN2002436
Belotti, Paganoni, Manenti, Garofalo, Marchini, Taraboletti, Giavazzi: Matrix metalloproteinases (MMP9 and MMP2) induce the release of vascular endothelial growth factor (VEGF) by ovarian carcinoma cells: implications for ascites formation. in Cancer research 2003
Show all 3 references for ABIN2002436
Mouse (Murine) MMP8 Protein expressed in Human Cells - ABIN2007891
Mira, Lacalle, Buesa, de Buitrago, Jiménez-Baranda, Gómez-Moutón, Martínez-A, Mañes: Secreted MMP9 promotes angiogenesis more efficiently than constitutive active MMP9 bound to the tumor cell surface. in Journal of cell science 2004
Show all 3 references for ABIN2007891
Mouse (Murine) MMP8 Protein expressed in CHO Cells - ABIN2007889
Ram, Sherer, Shoenfeld: Matrix metalloproteinase-9 and autoimmune diseases. in Journal of clinical immunology 2006
Show all 3 references for ABIN2007889
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 Proteins) and therefore increasing the bioavailability of TGF-beta (show TGFB1 Proteins).
MMP-8-deficient mice had significantly lower serum triglyceride (TG) levels (P = 0.003) and larger HDL (show APOA Proteins)particles compared with wild-type (WT (show HSD11B1 Proteins)) mice. However, no differences were observed in the apoA-I levels.
These results demonstrate that MMP-8 critically mediates microglial activation by modulating TNF-alpha (show TNF Proteins) activity, which may explain neuroinflammation in septic mouse brain.
MMP-13 (show MMP13 Proteins) prevails over MMP-8 in collagen degradation in atheromata.
MMP8 enhances vascular smooth muscle cell proliferation via an ADAM10 (show ADAM10 Proteins), N-cadherin (show CDH2 Proteins), and beta-catenin (show CTNNB1 Proteins)-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.
These results show that MMP-8 can modulate the levels of S100A8 (show S100A8 Proteins) and S100A9 (show S100A9 Proteins) and its absence promotes the lung inflammatory response during endotoxemia.
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 Proteins) and serum in women with polycystic ovary syndrome, and is potentiated in the presence of gingivitis
Positive results of the aMMP-8 test significantly correlate with generalized ChP (show CHP Proteins). The aMMP-8 test may be used by physicians to detect periodontitis in their patients.
miR (show MLXIP Proteins)-539 plays a key role in inhibiting osteosarcoma cell invasion and migration and can regulate MMP8 expression in osteosarcoma cells.
salivary levels of the analyzed biomarkers MMP-8, -9, MPO (show MPO Proteins) are associated with periodontal status. However, these biomarkers could not differentiate between patients with or without a MI.
Moderate-strength STS (show STS Proteins) causes the highest TIMP-1 (show TIMP1 Proteins)/MMP-8 ratio, leading to appropriate conditions for reformation of the extracellular matrix
Gender-specific analysis of MMPs demonstrated consistent increase in MMP-1 (show MMP1 Proteins) and -8 in tuberculosis, but MMP-8 was a better discriminator for TB in men.
MMP-8, MMP-9 (show MMP9 Proteins), and YKL-40 (show CHI3L1 Proteins) might serve as novel non-invasive biomarkers of CF lung disease and pulmonary exacerbations.
The expression of MMP-7 (show MMP7 Proteins), -8, -9 and -13 in the gingiva of the young patients with aggressive periodontitis and type 1 diabetes mellitus was positive in all studied cases.
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)