MAB3329
Anti-MMP-14 Antibody, catalytic domain, clone LEM-2/63.1
clone LEM-2/63.1, Chemicon®, from mouse
Synonym(s):
MT1-MMP
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Pricing and availability is not currently available.
Recommended Products
biological source
mouse
Quality Level
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
LEM-2/63.1, monoclonal
species reactivity
mouse
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
immunoprecipitation (IP): suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... MMP14(4323)
Related Categories
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.
Specificity
LEM-2/63.1 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.
Application
Anti-MMP-14 Antibody, catalytic domain, clone LEM-2/63.1 detects level of MMP-14 & has been published & validated for use in ELISA, IP & WB.
Western Blot
Immunohistochemistry: Frozen sections
Immunofluorescence
Immunoprecipitation
Flow Cytometry
Blocking
Optimal working dilutions must be determined by the end user.
Immunohistochemistry: Frozen sections
Immunofluorescence
Immunoprecipitation
Flow Cytometry
Blocking
Optimal working dilutions must be determined by the end user.
Physical form
Format: Purified
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
Not finding the right product?
Try our Product Selector Tool.
recommended
Product No.
Description
Pricing
Storage Class Code
10 - 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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Membrane localization of membrane type 1 matrix metalloproteinase by CD44 regulates the activation of pro-matrix metalloproteinase 9 in osteoclasts.
Chellaiah, MA; Ma, T
BioMed Research International null
The membrane type matrix metalloproteinase MMP14 mediates constitutive shedding of MHC class I chain-related molecule A independent of A disintegrin and metalloproteinases.
Liu, G; Atteridge, CL; Wang, X; Lundgren, AD; Wu, JD
Journal of immunology (Baltimore, Md. : 1950) (1950)
Ursula Hiden et al.
The American journal of pathology, 182(5), 1563-1571 (2013-03-09)
Fetal growth restriction (FGR) results from placental insufficiency to adequately supply the fetus. This insufficiency involves impaired cytotrophoblast functions, including reduced migration and invasion, proliferation, and syncytium formation. Membrane-type matrix metalloproteinase 1 (MT1-MMP) is a key enzyme in these cellular
Adekunle Alabi et al.
Nature communications, 12(1), 1889-1889 (2021-03-27)
Plasma low-density lipoprotein (LDL) is primarily cleared by LDL receptor (LDLR). LDLR can be proteolytically cleaved to release its soluble ectodomain (sLDLR) into extracellular milieu. However, the proteinase responsible for LDLR cleavage is unknown. Here we report that membrane type
Megan I Brasher et al.
Molecular cancer research : MCR, 20(3), 434-445 (2021-12-09)
Invasion of neighboring extracellular matrix (ECM) by malignant tumor cells is a hallmark of metastatic progression. This invasion can be mediated by subcellular structures known as invadopodia, the function of which depends upon soluble N-ethylmaleimide-sensitive factor-activating protein receptor (SNARE)-mediated vesicular
Active Filters
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service
