Skip to Content
Merck
All Photos(1)

Key Documents

MAB3329

Sigma-Aldrich

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


About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

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)

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.

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.

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.

Visit 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)
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
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
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

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