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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. De plus, nous expédions Matrix Metallopeptidase 10 (Stromelysin 2) Kits (84) et Matrix Metallopeptidase 10 (Stromelysin 2) Protéines (13) et beaucoup plus de produits pour cette protéine.
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Human Polyclonal MMP10 Primary Antibody pour 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. dans Biology of reproduction 2012
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Human Polyclonal MMP10 Primary Antibody pour WB - ABIN966586
Muller, Quantin, Gesnel, Millon-Collard, Abecassis, Breathnach: The collagenase gene family in humans consists of at least four members. dans The Biochemical journal 1988
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Human Polyclonal MMP10 Primary Antibody pour 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. dans PLoS ONE 2013
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Human Polyclonal MMP10 Primary Antibody pour WB - ABIN517967
Teng, Wang, Hood, Conrads, Hamilton, Maxwell, Darcy, Conrads: Identification of candidate circulating cisplatin-resistant biomarkers from epithelial ovarian carcinoma cell secretomes. dans 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 (Montrer CXCR4 Anticorps)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 (Montrer CXCR4 Anticorps)/SDF1 (Montrer CXCL12 Anticorps) 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 (Montrer PMP22 Anticorps)) treatment, and conclude MMP10 is required for resolution of DSS (Montrer PMP22 Anticorps)-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 (Montrer FGA Anticorps) 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 (Montrer MMP7 Anticorps), MMP-10 and TIMP-1 (Montrer TIMP1 Anticorps) correlated with clinicopathologic features. We suggest that these genes may play a role during progression of the disease MMP-10, MMP-7 (Montrer MMP7 Anticorps), TIMP-1 (Montrer TIMP1 Anticorps), TIMP-2 (Montrer TIMP2 Anticorps) 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 (Montrer TGFB1 Anticorps) stimulates HSC-4 cell invasion through the Slug/Wnt-5b (Montrer WNT5B Anticorps)/MMP-10 signalling axis.
the rs17435959 polymorphism of the MMP-10 gene may be associated with an increased risk of pelvic organ prolapse (POP (Montrer PREP Anticorps)).
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 (Montrer MMP3 Anticorps)), transforming growth factor beta 1 (TGFbeta1 (Montrer TGFB1 Anticorps)) and collagen type X alpha I (COL10A1 (Montrer COL10A1 Anticorps)) gene polymorphisms with traits related to leg weakness in pigs.
the identification of MMP1 (Montrer MMP1 Anticorps) and MMP10 genes in swine is reported.
contribution of MMPs to the inflammatory breakdown of the blood-CSF (Montrer CSF2 Anticorps) barrier in vitro
Results indicate that leukemia inhibitory factor (LIF (Montrer LIF Anticorps)) and Oncostatin M (Montrer OSM Anticorps) increase the expression of MMP-1 (Montrer MMP1 Anticorps), MMP-3 (Montrer MMP3 Anticorps), and TIMP-1 (Montrer TIMP1 Anticorps) several fold, and that their expression is reduced to basal levels in the presence of the LIF (Montrer LIF Anticorps) 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