MAB3328
Anti-MMP-14 Antibody, catalytic domain, clone LEM-2/15.8
clone LEM-2/15.8, Chemicon®, from mouse
Synonym(s):
MT1-MMP
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
LEM-2/15.8, monoclonal
species reactivity
mouse, human
packaging
antibody small pack of 25 μg
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG1κ
NCBI accession no.
UniProt accession no.
shipped in
ambient
storage temp.
2-8°C
target post-translational modification
unmodified
Gene Information
human ... MMP14(4323)
General description
MT1-MMP plays an important role during endothelial cell migration and matrix remodeling. Although the role of MT1-MMP in endothelial cell motility is not fully characterized, its activity appears to modulate endothelial migration, invasion, and formation of capillary tubes during the angiogenic response (Galvez, 2001). Mt1-MMP also appears to play a key role in monocyte revruitment during inflammation (Salomon, 2005).
Specificity
LEM-2/15.8 reacts with human MT1-MMP and displays crossreactivity with mouse specimens. This antibody was generated against the catalytic domain of MT1-MMP and is able to inhibit enzyme activity.
Immunogen
Epitope: catalytic domain
Synthetic peptide: amino acid sequence 218-233 within the catalytic domain
Application
Detect MMP-14 using this Anti-MMP-14 Antibody, catalytic domain, clone LEM-2/15.8 validated for use in ELISA, IP & WB.
Research Category
Cell Structure
Cell Structure
Research Sub Category
MMPs & TIMPs
MMPs & TIMPs
Western Blot
Immunohistochemistry: Frozen and paraffin-embedded tissues
Immunofluorescence
Flow Cytometry
Blocking: 10-15μg/mL
Optimal working dilutions must be determined by the end user.
Immunohistochemistry: Frozen and paraffin-embedded tissues
Immunofluorescence
Flow Cytometry
Blocking: 10-15μg/mL
Optimal working dilutions must be determined by the end user.
Physical form
Format: Purified
Purified immunoglobulin by Protein A chromatography . Liquid in 0.2M phosphate, 0.25M NaCl, pH 7.6, containing 0.1% sodium azide.
Storage and Stability
Maintain at 2° to 8°C for up to 12 months from date of receipt.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Description
Pricing
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 2
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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Charles Marusak et al.
Pharmacological research, 113(Pt A), 515-520 (2016-10-21)
MT1-MMP and MMP2 have been implicated as pro-tumorigenic and pro-metastatic factors in a wide variety of cancers including melanoma. We have previously demonstrated that MT1-MMP is highly expressed in melanoma where it promotes melanoma cell invasion and metastasis in part
J K Björk et al.
Oncogene, 35(14), 1770-1784 (2015-06-30)
Heat-shock factors (HSFs) are key transcriptional regulators in cell survival. Although HSF1 has been identified as a driver of carcinogenesis, HSF2 has not been explored in malignancies. Here, we report that HSF2 suppresses tumor invasion of prostate cancer (PrCa). In
G Daniel Grass et al.
Journal of cell science, 125(Pt 3), 777-788 (2012-03-06)
A defining feature of malignant tumor progression is cellular penetration through the basement membrane and interstitial matrices that separate various cellular compartments. Accumulating evidence supports the notion that invasive cells employ specialized structures termed invadopodia to breach these structural barriers.
Karina Di Gregoli et al.
Arteriosclerosis, thrombosis, and vascular biology, 34(9), 1990-2000 (2014-07-06)
Our recent studies have highlighted membrane type-1 matrix metalloproteinase (MMP)-14 as a selective marker for an invasive subset of macrophages potentially related to atherosclerotic plaque progression. Moreover, colony stimulating factors (CSF) may exert divergent effects on macrophage MMP expression, possibly
Susan H Taylor et al.
eLife, 4, e09345-e09345 (2015-09-22)
Type I collagen-containing fibrils are major structural components of the extracellular matrix of vertebrate tissues, especially tendon, but how they are formed is not fully understood. MMP14 is a potent pericellular collagenase that can cleave type I collagen in vitro.
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