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AB8345

Sigma-Aldrich

Anti-MMP-14 Antibody

serum, Chemicon®

Synonym(s):

MT1-MMP

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About This Item

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

biological source

rabbit

Quality Level

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable
flow cytometry: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... MMP14(4323)

Specificity

The antibody recognizes native and recombinant proteins.

Immunogen

Catalytic domain of MT1-MMP

application

Anti-MMP-14 Antibody detects level of MMP-14 & has been published & validated for use in ELISA, FC, IP, WB & IC.
Immunocytochemistry: 5-10 μg / ml

Western blot: 5 μg / ml Expected band sizes: 60-63 kDA and 42 kDa pro-enzyme and degradation form respectively.

Immunopreciptation: 1-2 μg / mg total protein in 500 μl reaction volume.

FACS Analysis: 5 μg/ mL (1 million cells per mL)

EIA: 1:10,000

Optimal working dilutions must be determined by the end user.
Research Category
Cell Structure
Research Sub Category
MMPs & TIMPs

Physical form

Liquid in PBS, pH 7.6, containing 0.01% sodium azide as a preservative.

Storage and Stability

Store antibody at -20°C for 12 months. Avoid repeat freeze thaw cycles.

Analysis Note

Control
Immunocytochemistry positive control: U251 glioma cells; negative control MCF7 breast carcinoma.

Western Blot positive control: HT1080 fibrosarcoma, negative control: MCF7 breast carcinoma

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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Storage Class

10 - Combustible liquids

wgk_germany

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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Albert G Remacle et al.
Oncotarget, 8(2), 2781-2799 (2016-11-12)
The invasion-promoting MT1-MMP is a cell surface-associated collagenase with a plethora of critical cellular functions. There is a consensus that MT1-MMP is a key protease in aberrant pericellular proteolysis in migrating cancer cells and, accordingly, a promising drug target. Because
David Alonso-Escolano et al.
British journal of pharmacology, 141(2), 241-252 (2003-12-24)
1. Matrix metalloproteinase-2 (MMP-2) plays a role in agonist- and tumour cell-induced platelet aggregation (TCIPA). 2. MMP-2 is synthesized as a proenzyme and is activated at the cell surface by membrane type-1 matrix metalloproteinase (MT1-MMP, MMP-14). 3. The significance of
Caveolin-1 mediates the expression and localization of cathepsin B, pro-urokinase plasminogen activator and their cell-surface receptors in human colorectal carcinoma cells.
Cavallo-Medved, D; Mai, J; Dosescu, J; Sameni, M; Sloane, BF
Journal of Cell Science null
Albert G Remacle et al.
The Journal of biological chemistry, 288(28), 20568-20580 (2013-06-05)
Proteolytic activity of cell surface-associated MT1-matrix metalloproteinase (MMP) (MMP-14) is directly related to cell migration, invasion, and metastasis. MT1-MMP is regulated as a proteinase by activation and conversion of the latent proenzyme into the active enzyme, and also via inhibition
Mengying Xing et al.
iScience, 27(2), 108840-108840 (2024-02-02)
N-α-acetyltransferase D (NatD) mediates N-α-terminal acetylation of histone H4 (Nt-Ac-H4), but its role in breast cancer metastasis remains unknown. Here, we show that depletion of NatD directly represses the expression of FOXA2, and is accompanied by a significant reduction in

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