Render Target: STATIC
Render Timestamp: 2024-10-04T10:07:40.802Z
Commit: f04ddd7fea9fb3592f59f61482fcb94610d25cbe
1% for the planet logo
PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

MT1-MMP (E3S5S) Rabbit mAb #26424

Filter:
  • WB
  • IHC

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 62
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IHC-Immunohistochemistry 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunohistochemistry (Paraffin) 1:50 - 1:200

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    MT1-MMP (E3S5S) Rabbit mAb recognizes endogenous levels of total MT1-MMP protein. This antibody cross-reacts with a band at 135 kDa of unknown origin.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a recombinant fragment of human MT1-MMP protein.

    Background

    The matrix metalloproteinase (MMP) family of proteases are a group of zinc-dependent enzymes that target extracellular proteins, including growth factors, cell surface receptors, adhesion molecules, and other proteases (1). Matrix metalloproteinases can be broadly categorized based on function and cellular localization, and include six distinct membrane-type (MT) metalloproteinases that share a transmembrane domain and short cytoplasmic tail (2). Membrane type-1 matrix metalloproteinase (MT1-MMP, MMP14) is involved in regulating development, angiogenesis, tissue remodeling, and tumor progression (3-6). MT1-MMP and other metalloproteinases promote tumor cell invasion by accumulating in specialized structures known as invadopodia, which remodel the ECM and allow tumor cells to breach the basement membrane (7). The abundance and presence of MT1-MMP at the cell surface is controlled by targeted endocytosis, which may be regulated by the MT1-MMP cytoplasmic domain (8). MT1-MMP protease activity can be further regulated through homodimer formation, autocatalytic processing, domain shedding, and the interaction with inhibitory proteins. Activation of the MT1-MMP proenzyme results from cleavage of full-length MT1-MMP by furin in the trans-Golgi network, which removes the inhibitory propeptide domain (9). At the cell surface, MT1-MMP can be found in a protein complex with the soluble metalloproteinase MMP2 and the MMP inhibitor TIMP2. MT1-MMP mediated cleavage and activation of MMP2 generate the active MMP2 collagenase, which plays important roles in ECM remodeling and tumor invasion (10). MT1-MMP interacts with a large number of substrates in addition to MMP2, including interstitial collagens, adhesive glycoproteins (i.e., laminin), and cell surface receptors (11).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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