AB6004
Anti-MT1-MMP Antibody, hinge region
from rabbit, purified by affinity chromatography
Synonym(s):
MT-MMP 1, Membrane-type matrix metalloproteinase 1, Membrane-type-1 matrix metalloproteinase, matrix metallopeptidase 14 (membrane-inserted), matrix metalloproteinase 14, matrix metalloproteinase 14 (membrane-inserted), membrane type 1 metalloprotease
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All Photos(3)
About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
rabbit
Quality Level
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
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.
Specificity
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.
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).
Quality
Evaluated on a representative lot by Western blot on rat lung lysate using Anti-MT1-MMP.
Target description
~ 65 kDa
Linkage
Replaces: AB815
Analysis Note
Control
Rat lung lysate.
Rat lung lysate.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
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Product No.
Description
Pricing
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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
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
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
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
N Akanuma et al.
British journal of cancer, 110(1), 189-198 (2013-11-08)
FSCN1 and matrix metalloproteinase 14 (MMP14) are both invadopodia-related proteins. We herein elucidate the tumourigenicity of these proteins and identify novel therapeutic agents in esophageal squamous cell carcinoma (ESCC). FSCN1 and MMP14 were evaluated by immunohistochemistry and quantitative PCR, and
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