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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 art. Zusätzlich bieten wir Ihnen Matrix Metallopeptidase 10 (Stromelysin 2) Antikörper (168) und Matrix Metallopeptidase 10 (Stromelysin 2) Proteine (13) und viele weitere Produktgruppen zu diesem Protein an.
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Human MMP10 ELISA Kit für Sandwich ELISA - ABIN625052
Lisboa, Andrade, Cunha-Melo: Toll-like receptor activation and mechanical force stimulation promote the secretion of matrix metalloproteinases 1, 3 and 10 of human periodontal fibroblasts via p38, JNK and NF-kB. in Archives of oral biology 2013
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Mouse (Murine) MMP10 ELISA Kit für Sandwich ELISA - ABIN415613
Justilien, Regala, Tseng, Walsh, Batra, Radisky, Murray, Fields: Matrix metalloproteinase-10 is required for lung cancer stem cell maintenance, tumor initiation and metastatic potential. in PLoS ONE 2012
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Human MMP10 ELISA Kit für Sandwich ELISA - ABIN414817
Mern, Fontana, Beierfuß, Thomé, Hegewald et al.: A combinatorial relative mass value evaluation of endogenous bioactive proteins in three-dimensional cultured nucleus pulposus cells of herniated intervertebral discs: identification of potential ... in PLoS ONE 2013
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De Abrew, Thomas-Virnig, Rasmussen, Bolterstein, Schlosser, Allen-Hoffmann: TCDD induces dermal accumulation of keratinocyte-derived matrix metalloproteinase-10 in an organotypic model of human skin. in Toxicology and applied pharmacology 2014
Rat (Rattus) MMP10 ELISA Kit für Sandwich ELISA - ABIN416349
Wei, Cui, Lainscak, Zhang, Li, Huang, Zhang, Zheng, Hu: Type-specific dysregulation of matrix metalloproteinases and their tissue inhibitors in end-stage heart failure patients: relationship between MMP-10 and LV remodelling. in Journal of cellular and molecular medicine 2011
These results indicate that MMP10 serves a beneficial role in response to acute infection by moderating the proinflammatory response of resident and infiltrating macrophages.
MMP-10 facilitates the clearance of multiwalled carbon nanotubesand moderates the pro-inflammatory response of exposed alveolar and infiltrated macrophages.
crosstalk between MMP10 and the CXCR4/SDF1 axis contributes to hepatocarci (zeige CXCR4 ELISA Kits)nogenesis
Matrix metalloproteinase-10 expression is induced during hepatic injury and plays a fundamental role in liver tissue repair.
our findings support a model in which MMP-10 activity modulates CXCR4 (zeige CXCR4 ELISA Kits)/SDF1 (zeige CXCL12 ELISA Kits) signaling, which is essential for efficient skeletal muscle regeneration.
Dissection of the matrix metalloproteinase 10 (MMP10) substrate degradome in fibroblast secretomes.
Thus, our findings indicate that MMP-10 is critical for skeletal muscle maintenance and regeneration during injury and disease.
MMP10 promotes macrophage movement
Assessed MMP-10's role in a murine model of colonic tissue damage induced by dextran sulfate sodium(DSS (zeige PMP22 ELISA Kits)) treatment, and conclude MMP10 is required for resolution of DSS (zeige PMP22 ELISA Kits)-induced colonic damage, and in its absence, chronic inflammation and dysplasia occurs.
Mmp10 is required for maintenance of a highly tumorigenic, cancer-initiating, metastatic stem-like cell population in lung cancer.
There is a significant association in the expression of P-Rex1 (zeige PREX1 ELISA Kits) and MMP10 in human luminal breast cancer, and their co-expression is indicative of poor prognosis.
MMP10 is a novel marker for cancer stem-like cells (CSCs)/cancer-initiating cells in epithelial ovarian cancer
Data show that AJUBA upregulated MMP10 and MMP13 (zeige MMP13 ELISA Kits) expression in esophageal squamous cell carcinoma (ESCC).
MMP10 is overexpressed in the serum and pulmonary arteries of patients with systemic sclerosis-associated pulmonary hypertension.
Using a quantum chemical approach method, it has been established that mutations in MMP-10 and FGA (zeige FGA ELISA Kits) proteins led to substantial energetic modifications suggesting an impact on their functions and/or stability in the recurrent pregnancy loss patients.
We conclude that in the resected esophageal cancer an increased mRNA expression of MMP-7 (zeige MMP7 ELISA Kits), MMP-10 and TIMP-1 (zeige TIMP1 ELISA Kits) correlated with clinicopathologic features. We suggest that these genes may play a role during progression of the disease MMP-10, MMP-7 (zeige MMP7 ELISA Kits), TIMP-1 (zeige TIMP1 ELISA Kits), TIMP-2 (zeige TIMP2 ELISA Kits) were overexpressed in 73%, 85%, 55% and 42% of esophageal cancer samples, respectively.
Mycobacterium tuberculosis activates inflammatory and stromal cells to secrete MMP-10, and this is partly driven by the virulence factor early secretory antigenic target-6.
MMP10 expression is significantly upregulated in human masticatory mucosa during wound healing.
Our results suggest that the level of the MMP-10 expression in tumor epithelium of cutaneous squamous cell carcinoma and basal cell carcinoma may contribute to the different invasive patterns observed in these tumors
The present study was aimed to determine the association between metalloproteinase 3 (MMP3 (zeige MMP3 ELISA Kits)), transforming growth factor beta 1 (TGFbeta1 (zeige TGFB1 ELISA Kits)) and collagen type X alpha I (COL10A1 (zeige COL10A1 ELISA Kits)) gene polymorphisms with traits related to leg weakness in pigs.
the identification of MMP1 (zeige MMP1 ELISA Kits) and MMP10 genes in swine is reported.
contribution of MMPs to the inflammatory breakdown of the blood-CSF (zeige CSF2 ELISA Kits) barrier in vitro
Results indicate that leukemia inhibitory factor (LIF (zeige LIF ELISA Kits)) and Oncostatin M (zeige OSM ELISA Kits) increase the expression of MMP-1 (zeige MMP1 ELISA Kits), MMP-3 (zeige MMP3 ELISA Kits), and TIMP-1 (zeige TIMP1 ELISA Kits) several fold, and that their expression is reduced to basal levels in the presence of the LIF (zeige LIF ELISA Kits) antagonist MH35-BD.
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 and fibronectin. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
matrix metalloproteinase 10
, matrix metalloproteinase-10
, stromelysin 2
, matrix metalloprotease 10
, matrix metalloproteinase 10 (stromelysin 2)
, transin 2
, transformation-associated protein 34A
, matrix metalloproteinase 3