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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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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Find documentation for the products that you have recently purchased in the Document Library.
VANGL2 regulates membrane trafficking of MMP14 to control cell polarity and migration.
Williams, BB; Cantrell, VA; Mundell, NA; Bennett, AC; Quick, RE; Jessen, JR
Journal of Cell Science null
Sodium fluoride induces podosome formation in endothelial cells.
Tatin, Florence, et al.
Biology of the Cell, 102, 489-498 (2010)
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
Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573: role in endothelial and tumor cell migration.
Nyalendo, C; Michaud, M; Beaulieu, E; Roghi, C; Murphy, G; Gingras, D; Beliveau, R
The Journal of Biological Chemistry null
KIF5B and KIF3A/KIF3B kinesins drive MT1-MMP surface exposure, CD44 shedding, and extracellular matrix degradation in primary macrophages.
Wiesner, Christiane, et al.
Blood, 116, 1559-1569 (2010)
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