biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
purified by
affinity chromatography
species reactivity
human, rat
technique(s)
immunohistochemistry: suitable (paraffin), western blot: suitable
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Quality Level
Gene Information
human ... MMP14(4323)
General description
Matrix metalloproteinases (MMPs) are a family of secreted and membrane-bound zinc endopeptidases. Collectively, these enzymes degrade the components of extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. MMPs play an important role in wound healing, apoptosis, bone elongation, embryo development, angiogenesis, cancer metastases, and tissue remodeling within many disease states.
Most MMP′s are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, MT1-MMP (MMP-14) is a member of the membrane-type subfamily. Each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. MT1-MMP is capable of mediating pericellular proteolysis of extracellular matrix components and is therefore thought to be an important molecular tool for cellular remodeling of the surrounding matrix. This protein also activates MMP2 protein, and this activity may be involved in tumor invasion.
Most MMP′s are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, MT1-MMP (MMP-14) is a member of the membrane-type subfamily. Each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. MT1-MMP is capable of mediating pericellular proteolysis of extracellular matrix components and is therefore thought to be an important molecular tool for cellular remodeling of the surrounding matrix. This protein also activates MMP2 protein, and this activity may be involved in tumor invasion.
~ 65 kDa
Immunogen
KLH conjugated synthetic peptide selected from the hinge region of human MT1-MMP.
Application
Detect MT1-MMP using this Anti-MT1-MMP Antibody, hinge region validated for use in WB, IH(P).
Biochem/physiol Actions
Predicted to cross react with mouse, (95% sequence homology) and monkey chimpanzee, canine and bovine (100% sequence homology). Reactivity with other species has not been tested.
The antibody recognizes human and rat MT1-MMP. It does not cross react with MMP-1, MMP-2, MMP-8, MMP-9, and MMP-13.
Analysis Note
Control
Rat lung lysate.
Rat lung lysate.
Evaluated on a representative lot by Western blot on rat lung lysate using Anti-MT1-MMP.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Replaces: AB815
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存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Mario A Cepeda et al.
Molecular cancer, 15(1), 65-65 (2016-10-21)
Membrane Type-1 Matrix Metalloproteinase (MT1-MMP) is a multifunctional protease implicated in metastatic progression ostensibly due to its ability to degrade extracellular matrix (ECM) components and allow migration of cells through the basement membrane. Despite in vitro studies demonstrating this principle
Juhyeon Son et al.
Journal of biochemical and molecular toxicology, 35(10), e22868-e22868 (2021-08-03)
Osteosarcoma (OS) is a primary bone neoplasm that is highly malignant. As advances in chemotherapy for the treatment of OS have stagnated, discovery of new reagents is required. Emetine is a phytochemical which can be isolated from a medicinal herb Cephaelis
Yuko Matsuura-Hachiya et al.
Biochemistry and biophysics reports, 4, 180-186 (2015-09-21)
The renin-angiotensin system is known to be involved in skin remodeling and inflammation. Previously, we reported that ultraviolet B (UVB) irradiation enhanced angiotensin-converting enzyme (ACE) expression and angiotensin II levels in hairless mouse skin, and an ACE inhibitor, enalapril maleate
J A Willson et al.
Journal of cell communication and signaling, 12(2), 479-488 (2017-08-30)
The membrane bound matrix metalloproteinase MT1-MMP plays roles in modulating cell movement, independent of its abilities to remodel the extracellular matrix. Unlike many MMPs, MT1-MMP is activated in the Golgi prior to secretion by a pro-protein convertase, primarily furin. Regulation
Immunolocalization of membrane-type 1 MMP in human rheumatoid synovium tissues.
Qin, S; Wang, F; Zhou, M; Ding, W; Chen, L; Lu, Y
International Journal of Clinical and Experimental Pathology null
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