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MMP7 shedding of syndecan-1 (show SDC1 Proteins)/CXCL1 (show CXCL1 Proteins) complexes functions as a checkpoint that restricts neutrophil activation at sites of epithelial injury.
MMP7 exerts a restrictive role on H. pylori-induced gastric injury and the development of premalignant lesions by suppressing M1 macrophage polarization.
absence of MMP7 protects mice from LPS (show TLR4 Proteins)-induced intestinal permeability and lethality.
regulator of beta-catenin (show CTNNB1 Proteins) function in injured lung epithelium
Angiotensin II suppresses RECK (show RECK Proteins), but induces matrix metalloproteinases both in vivo and in vitro.
MMP7 regulated ciliated cell formation.
SPARC (show SPARC Proteins) suppresses angiogenesis of gastric cancer by down-regulating the expression of VEGF (show VEGFA Proteins) and MMP-7
Protein expression levels of MMP-7, MMP-14 and ERK1/2 phosphorylation level were all elevated with the increasing pathological grades in brain glioma tissues.
levels of renal MMP-7 correlate with Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) activity.
STAT3 (show STAT3 Proteins) plays an important role in regulation of tumor growth, invasion, and angiogenesis, which could be act by reducing MMP-7 expression in pancreatic cancer cells.
Studies have identified an unexpected tumor-suppressive role for host-derived MMP-7 in myeloma bone disease in vivo, and highlight the importance of elucidating the effect of individual MMPs in a disease-specific context.
the crosstalk between ARF and MMP7 in nucleus contributes to ECM (show MMRN1 Proteins) network in tumor microenvironments in vivo, implicating a novel therapeutic target for advanced PCa (show FLVCR1 Proteins) treatment.
Data suggest that HAI1 (show SPINT1 Proteins), a protease on the surface of colon carcinoma cells, is an MMP7 substrate; proteolysis by MMP7 releases extracellular region as soluble HAI1 (show SPINT1 Proteins) (sHAI1); sHAI1 induces cancer cell aggregation; cholesterol sulfate is required for MMP-7--catalyzed generation of sHAI1. (HAI1 (show SPINT1 Proteins) = hepatocyte growth factor activator inhibitor type 1 (show SPINT1 Proteins); MMP7 = matrix metalloproteinase-7)
Results indicate that the matrix metallopeptidase 7 (MMP7)A-181G genotype interacts with age and gender and may serve as an early and predictive biomarker for childhood acute lymphoblastic leukemia (ALL).
The A/A genotype (OR=0.120) and A allele (OR=0.442) reduce the risk of recurrent depressive disorder occurrence in the examined polymorphisms for MMP-2 (show MMP2 Proteins), MMP-7 and MMP-9 (show MMP9 Proteins).
SLC12A5 (show SLC12A5 Proteins) promoted the migration and invasion of BUC by enhancing MMP-7 expression.
Overexpression of LAMC2 (show LAMC2 Proteins) and knockdown of CD82 (show CD82 Proteins) markedly promoted GC cell invasion and activated EGFR (show EGFR Proteins)/ERK1/2-MMP7 signaling via upregulation of the expression of phosphorylated (p)-EGFR (show EGFR Proteins), p-ERK1/2 and MMP7.
Matrix Metalloproteinase-7 Promoter polymorphism is associated with breast Cancer.
Data suggest that the cytoplasmic domain of Sdc2 (show SDC2 Proteins) is involved in regulation of expression of MMP7 in colon carcinoma/adenocarcinoma cells; induction of MMP7 involves protein kinase C gamma (show PRKCG Proteins)-mediated FAK (show PTK2 Proteins)/ERK (show EPHB2 Proteins) signaling. (Sdc2 (show SDC2 Proteins) = syndecan-2 (show SDC2 Proteins); MMP7 = matrix metalloproteinase-7; FAK (show PTK2 Proteins) = focal adhesion kinase 1 (show PTK2 Proteins))
We conclude that in the resected esophageal cancer an increased mRNA expression of MMP-7, MMP-10 (show MMP10 Proteins) and TIMP-1 (show TIMP1 Proteins) correlated with clinicopathologic features. We suggest that these genes may play a role during progression of the disease MMP-10 (show MMP10 Proteins), MMP-7, TIMP-1 (show TIMP1 Proteins), TIMP-2 (show TIMP2 Proteins) were overexpressed in 73%, 85%, 55% and 42% of esophageal cancer samples, respectively.
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. The enzyme encoded by this gene degrades proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
, matrilysin, uterine
, matrix metalloproteinase 7
, matrix metalloproteinase-7
, pump-1 protease
, uterine metalloproteinase
, Matrix metalloproteinase 7 (matrilysin)
, matrix metalloproteinase 7 (matrilysin, uterine)
, uterine matrilysin
, matrilysin-related protein