产品名称
Anti-MMP-14 Antibody, catalytic domain, clone LEM-2/63.1, clone LEM-2/63.1, Chemicon®, from mouse
biological source
mouse
conjugate
unconjugated
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
Quality Level
Gene Information
human ... MMP14(4323)
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.
Biochem/physiol Actions
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.
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.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Physical form
Format: Purified
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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存储类别
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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)
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
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
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