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Merck

MAB3329

Anti-MMP-14 Antibody, catalytic domain, clone LEM-2/63.1

clone LEM-2/63.1, Chemicon®, from mouse

Synonyme(s) :

MT1-MMP

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A propos de cet article

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
LEM-2/63.1, monoclonal
Application:
ELISA, IP, WB
Citations:
9
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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)

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.

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.

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.

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

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wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

Classe de stockage

12 - Non Combustible Liquids


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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

Numéro d'article de commerce international

RéférenceGTIN
MAB332904053252724558

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