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MAB3329

Sigma-Aldrich

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

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

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别名:
MT1-MMP
UNSPSC代码:
12352203
eCl@ss:
32160702
NACRES:
NA.41

生物来源

mouse

质量水平

抗体形式

purified immunoglobulin

抗体产品类型

primary antibodies

克隆

LEM-2/63.1, monoclonal

种属反应性

mouse

制造商/商品名称

Chemicon®

技术

ELISA: suitable
immunoprecipitation (IP): suitable
western blot: suitable

NCBI登记号

UniProt登记号

运输

wet ice

靶向翻译后修饰

unmodified

基因信息

human ... MMP14(4323)

一般描述

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.

特异性

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.

应用

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.

外形

Format: Purified

其他说明

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

法律信息

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

WGK

WGK 2

闪点(°F)

Not applicable

闪点(°C)

Not applicable


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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
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
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

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