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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 MMP16 Kits (18) and MMP16 Proteins (10) and many more products for this protein.
Showing 10 out of 134 products:
Human Polyclonal MMP16 Primary Antibody for WB - ABIN1883195
Kurata, Maruyama, Kato, Sato, Yamamoto, Ozaki, Nitta, Nabeshima, Morita, Mizuno, Ito, Yuzawa, Matsuo: Tissue-type plasminogen activator deficiency attenuates peritoneal fibrosis in mice. in American journal of physiology. Renal physiology 2009
Human Polyclonal MMP16 Primary Antibody for IHC, IHC (p) - ABIN4334965
Stadler, Rexhepaj, Singan, Murphy, Pepperkok, Uhlén, Simpson, Lundberg: Immunofluorescence and fluorescent-protein tagging show high correlation for protein localization in mammalian cells. in Nature methods 2013
miR-155 contributed to the up-regulation of MMP-16, and MMP-16 further degraded aggrecan and collagen type II, leading to the dehydration and degeneration of intervertebral discs
Neuronal knockdown of MT3-MMP resulted in the accumulation of NgR1 (show NEUROG1 Antibodies) at the cell surface and reduced the accumulation of the NgR1 (show NEUROG1 Antibodies) cleavage fragment in medium conditioned by cortical neurons
Study demonstrates that MT3-MMP, is expressed in mesenchymal tissues of the skeleton and in peri (show POSTN Antibodies)-skeletal soft connective tissue; and MT3-MMP-deficient mice display growth inhibition tied to a decreased viability of mesenchymal cells in skeletal tissues.
Findings suggest that these MMP16 rs10090371, ADAMTS3 rs788935, TLL2 (show TLL2 Antibodies) rs10882807 and MMP9 (show MMP9 Antibodies) rs3918251 may be promising prognostic biomarkers for cutaneous melanoma specific survival (CMSS).
the present findings indicate that MT3-MMP is down-regulated in ESCC, which correlates to lymph node metastasis and poor survival of patients with this disease.
more severe intervertebral disc degeneration is correlated with higher matrix metallopeptidase 16
results suggest that miR (show MLXIP Antibodies)-145 functions as a tumor metastasis suppressor gene by down-regulating MMP16 and may be a potential target in osteosarcoma treatment
the results support a role for MMP16 in promoting invasive properties of the meningioma tumours
These results demonstrate that the MT3-MMP promoter is frequently hypermethylated in colorectal cancer and that downregulation of MT3-MMP may be important for cell migration in colorectal cancer.
MMP16 is a putative indicator of adverse melanoma prognosis.
Expression of MMP-16 in HTB9 and T24 cells increases following transforming growth factorbeta1 treatment.
E2F1 (show E2F1 Antibodies) acts as a transcriptional activator for MMPs and directly enhances MMP transcription by binding to E2F1 (show E2F1 Antibodies) binding sequences in the promoter, or indirectly activates MMPs (MMP-9 (show MMP9 Antibodies) and MMP-16)through enhanced Sp1 (show PSG1 Antibodies) and NF-kappa B (show NFKB1 Antibodies)
Matrix metalloproteinase 16 (MMP16) was a downstream target of miR (show MLXIP Antibodies)-146b-5p.
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 encoded protein activates MMP2 by cleavage. This gene was once referred to as MT-MMP2, but was renamed as MT-MMP3 or MMP16.
, MT-MMP 3
, Membrane type 3-MMP
, matrix metalloproteinase 16
, matrix metalloproteinase-16
, membrane-type matrix metalloproteinase 3
, membrane-type-3 matrix metalloproteinase
, Putative transmembrane protein C8orf57
, matrix metalloproteinase 16 (membrane-inserted)
, membrane type-matrix metalloproteinase