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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 MMP11 Kits (38) and MMP11 Proteins (11) and many more products for this protein.
Showing 10 out of 138 products:
Human Monoclonal MMP11 Primary Antibody for IHC (fro), IHC (p) - ABIN781659
Luo, Guérin, Ludwig, Stoll, Basset, Anglard: Transcriptional induction of stromelysin-3 in mesodermal cells is mediated by an upstream CCAAT/enhancer-binding protein element associated with a DNase I-hypersensitive site. in The Journal of biological chemistry 2000
Show all 2 references for ABIN781659
Human Polyclonal MMP11 Primary Antibody for WB - ABIN390135
Anglard, Melot, Guérin, Thomas, Basset: Structure and promoter characterization of the human stromelysin-3 gene. in The Journal of biological chemistry 1995
Show all 2 references for ABIN390135
Human Polyclonal MMP11 Primary Antibody for EIA, WB - ABIN358684
Basset, Bellocq, Wolf, Stoll, Hutin, Limacher, Podhajcer, Chenard, Rio, Chambon: A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas. in Nature 1991
Show all 2 references for ABIN358684
Results show that MMP-11 has a paracrine function during mammary gland development that might be harnessed to promote tumor progression, exposing a new link between development and malignancy.
point-out the paradoxical role of MMP11 in favoring the onset and growth of lung metastases but limiting lung foci number, and inhibiting the cancer cell dissemination to other organs
investigation of a potential role of MMP-11 in adipose tissue development
The increased levels of ST-3 in the thymus may be due to the presence of macrophages responsible for clearance of apoptotic cells
downregulated by deglycosylation of CD147 in hepatocarcinoma cells
These data together provide compelling evidence into the function of MMP-11 and suggest that MMP-11 act as a tumor lymphatic metastasis-associated gene.
These findings reveal that the tumor biological marker CD147 functionally mediates MMP-11, VEGF-A (show VEGFA Antibodies) expression and tumor lymphatic metastasis.
Mmp11 exhibits collagenolytic function against collagen VI under normal conditions.
Our study describes the identification of MMP11 as a novel broadly expressed tumor associated antigen as target candidate for cancer immunotherapy.
the data demonstrate that miR125a5p functions as a tumor suppressor gene and serves an important role in inhibiting osteosarcoma cell migration, invasion and EMT (show ITK Antibodies) by targeting MMP11.
MMP-11 overexpression is associated with aggressive tumor phenotype and unfavorable clinical outcome in urothelial carcinomas.
Our study established that high serum levels of MMP-11 are associated with poor clinical outcome and may serve as a prognostic biomarker in colon cancer patients.
Overexpression of MMP-11 was discovered in sera of cancer patients compared with normal control group as well as in multiple tumor tissue specimens, such as gastric cancer, breast cancer, and pancreatic cancer. At present, some evidence supports that MMP-11 may work as a significant tumor biomarker for early detection of cancer, tumor staging, prognostic analysis, monitoring recurrence [review]
Matrix metalloproteinase 11 has a role in degenerating intervertebral disc disease
combined effects of the MMP-11 gene polymorphisms and environmental carcinogens are related to an increased risk for the development of OSCC and may be a predictive factor for tumor lymph node metastasis in Taiwanese with OSCC
results indicated that both CD147 and MMP-11 may be involved in the progression of colorectal cancer, and they are potential prognostic factors and might become new therapeutic targets for CRC (show CALR Antibodies) patients
High Expression of Matrix Metalloproteinase-11 is associated with Cholangiocarcinoma.
study showed that plasma level of MMP-11 may be useful for assessment of the disease progression, especially lymph node metastasis, in patients with OSCC
MMP-14 (show MMP14 Antibodies) function might represent one critical regulatory mechanism to control the extent of pericellular MMP-11 bioavailability and protect cells from excessive/inappropriate MMP-11 function.
Transgenic tadpoles were prepared with an elastase promoter driving either the ST3 gene or the constitutively active form of Notch (show NOTCH1 Antibodies) (IC).
analysis of substrate specificity for stromelysin-3: alpha1-PI is unlikely to be a physiological substrate
ST3 regulates cell fate and tissue morphogenesis through direct or indirect extracellular matrix remodeling
Laminin receptor precursor cleavage by ST3 plays a role in both physiological and pathological processes.
thyroid hormone (show PTH Antibodies) regulation of Xenopus laevis Stromelysin-3 is mediated by a DNA element in the first intron
Mutational analysis of the cleavage of the cancer-associated laminin receptor by stromelysin-3 reveals the contribution of flanking sequences to site recognition and cleavage efficiency.
ST3 expression, in the absence of T3 hormone, caused significant muscle cell death in the tail of premetamorphic transgenic tadpoles
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 activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP's, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix.
, matrix metalloproteinase 11
, matrix metalloproteinase-11
, stromelysin 3
, Matrix metalloproteinase 11 (stromelysin 3)
, stromelysin III
, gene 14