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MAB3328

Sigma-Aldrich

Anti-MMP-14 Antibody, catalytic domain, clone LEM-2/15.8

clone LEM-2/15.8, Chemicon®, from mouse

Synonym(s):

MT1-MMP

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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-2/15.8, monoclonal

species reactivity

mouse, human

packaging

antibody small pack of 25 μg

manufacturer/tradename

Chemicon®

technique(s)

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

isotype

IgG1κ

NCBI accession no.

UniProt accession no.

shipped in

ambient

storage temp.

2-8°C

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 (Salomon, 2005).

Specificity

LEM-2/15.8 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.

Immunogen

Epitope: catalytic domain
Synthetic peptide: amino acid sequence 218-233 within the catalytic domain

Application

Detect MMP-14 using this Anti-MMP-14 Antibody, catalytic domain, clone LEM-2/15.8 validated for use in ELISA, IP & WB.
Research Category
Cell Structure
Research Sub Category
MMPs & TIMPs
Western Blot

Immunohistochemistry: Frozen and paraffin-embedded tissues

Immunofluorescence

Flow Cytometry

Blocking: 10-15μg/mL

Optimal working dilutions must be determined by the end user.

Physical form

Format: Purified
Purified immunoglobulin by Protein A chromatography . Liquid in 0.2M phosphate, 0.25M NaCl, pH 7.6, containing 0.1% sodium azide.

Storage and Stability

Maintain at 2° to 8°C for up to 12 months from date of receipt.

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

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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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’.

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VANGL2 regulates membrane trafficking of MMP14 to control cell polarity and migration.
Williams, BB; Cantrell, VA; Mundell, NA; Bennett, AC; Quick, RE; Jessen, JR
Journal of Cell Science null
Sodium fluoride induces podosome formation in endothelial cells.
Tatin, Florence, et al.
Biology of the Cell, 102, 489-498 (2010)
J K Björk et al.
Oncogene, 35(14), 1770-1784 (2015-06-30)
Heat-shock factors (HSFs) are key transcriptional regulators in cell survival. Although HSF1 has been identified as a driver of carcinogenesis, HSF2 has not been explored in malignancies. Here, we report that HSF2 suppresses tumor invasion of prostate cancer (PrCa). In
Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573: role in endothelial and tumor cell migration.
Nyalendo, C; Michaud, M; Beaulieu, E; Roghi, C; Murphy, G; Gingras, D; Beliveau, R
The Journal of Biological Chemistry null
KIF5B and KIF3A/KIF3B kinesins drive MT1-MMP surface exposure, CD44 shedding, and extracellular matrix degradation in primary macrophages.
Wiesner, Christiane, et al.
Blood, 116, 1559-1569 (2010)

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