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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) Kits (84) und Matrix Metallopeptidase 10 (Stromelysin 2) Proteine (13) und viele weitere Produktgruppen zu diesem Protein an.
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Human Polyclonal MMP10 Primary Antibody für ICC, IHC (fro) - ABIN315644
McCord, Li, Rosewell, Brännström, Curry: Ovarian expression and regulation of the stromelysins during the periovulatory period in the human and the rat. in Biology of reproduction 2012
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Human Polyclonal MMP10 Primary Antibody für WB - ABIN966586
Muller, Quantin, Gesnel, Millon-Collard, Abecassis, Breathnach: The collagenase gene family in humans consists of at least four members. in The Biochemical journal 1988
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Human Polyclonal MMP10 Primary Antibody für ICC, IHC (fro) - ABIN408044
Olivotto, Otero, Astolfi, Platano, Facchini, Pagani, Flamigni, Facchini, Goldring, Borzì, Marcu: IKKα/CHUK regulates extracellular matrix remodeling independent of its kinase activity to facilitate articular chondrocyte differentiation. in PLoS ONE 2013
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Human Polyclonal MMP10 Primary Antibody für WB - ABIN517967
Teng, Wang, Hood, Conrads, Hamilton, Maxwell, Darcy, Conrads: Identification of candidate circulating cisplatin-resistant biomarkers from epithelial ovarian carcinoma cell secretomes. in British journal of cancer 2014
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 Antikörper)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 Antikörper)/SDF1 (zeige CXCL12 Antikörper) 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 Antikörper)) treatment, and conclude MMP10 is required for resolution of DSS (zeige PMP22 Antikörper)-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.
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 Antikörper) 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 Antikörper), MMP-10 and TIMP-1 (zeige TIMP1 Antikörper) correlated with clinicopathologic features. We suggest that these genes may play a role during progression of the disease MMP-10, MMP-7 (zeige MMP7 Antikörper), TIMP-1 (zeige TIMP1 Antikörper), TIMP-2 (zeige TIMP2 Antikörper) 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
these results suggest that TGF-beta1 (zeige TGFB1 Antikörper) stimulates HSC-4 cell invasion through the Slug/Wnt-5b (zeige WNT5B Antikörper)/MMP-10 signalling axis.
the rs17435959 polymorphism of the MMP-10 gene may be associated with an increased risk of pelvic organ prolapse (POP (zeige PREP Antikörper)).
According to this study, the expression of ST-2 is associated with histopathological grade and tumor differentiation in head and neck squamous cell carcinomas.
The present study was aimed to determine the association between metalloproteinase 3 (MMP3 (zeige MMP3 Antikörper)), transforming growth factor beta 1 (TGFbeta1 (zeige TGFB1 Antikörper)) and collagen type X alpha I (COL10A1 (zeige COL10A1 Antikörper)) gene polymorphisms with traits related to leg weakness in pigs.
the identification of MMP1 (zeige MMP1 Antikörper) and MMP10 genes in swine is reported.
contribution of MMPs to the inflammatory breakdown of the blood-CSF (zeige CSF2 Antikörper) barrier in vitro
Results indicate that leukemia inhibitory factor (LIF (zeige LIF Antikörper)) and Oncostatin M (zeige OSM Antikörper) increase the expression of MMP-1 (zeige MMP1 Antikörper), MMP-3 (zeige MMP3 Antikörper), and TIMP-1 (zeige TIMP1 Antikörper) several fold, and that their expression is reduced to basal levels in the presence of the LIF (zeige LIF Antikörper) 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