Overview

  • Product name
    Anti-MMP14 antibody [LEM-2/63.1]
    See all MMP14 primary antibodies
  • Description
    Mouse monoclonal [LEM-2/63.1] to MMP14
  • Host species
    Mouse
  • Tested applications
    Suitable for: WB, IP, ELISA, IHC-Fr, Flow Cyt, Inhibition Assay, ICC/IFmore details
  • Species reactivity
    Reacts with: Mouse, Human
    Predicted to work with: Rat, Xenopus laevis, Macaque monkey
  • Immunogen

    Synthetic peptide: C-AEPWTVRNEDLNGNDI-C, corresponding to amino acids 218-233 within the catalytic domain of Human MMP14

Properties

Applications

Our Abpromise guarantee covers the use of ab78738 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB Use at an assay dependent concentration. Predicted molecular weight: 66 kDa.
IP Use at an assay dependent concentration.
ELISA Use at an assay dependent concentration.
IHC-Fr Use at an assay dependent concentration.
Flow Cyt Use at an assay dependent concentration.

ab170191 - Mouse monoclonal IgG2a, is suitable for use as an isotype control with this antibody.

 

Inhibition Assay Use at an assay dependent concentration.
ICC/IF Use at an assay dependent concentration.

Target

  • Function
    Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7.
  • Tissue specificity
    Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors.
  • Sequence similarities
    Belongs to the peptidase M10A family.
    Contains 4 hemopexin-like domains.
  • Domain
    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
  • Post-translational
    modifications
    The precursor is cleaved by a furin endopeptidase.
  • Cellular localization
    Membrane. Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
  • Information by UniProt
  • Database links
  • Alternative names
    • Matrix metallopeptidase 14 (membrane inserted) antibody
    • Matrix metalloproteinase 14 antibody
    • Matrix metalloproteinase-14 antibody
    • Membrane type 1 matrix metalloproteinase antibody
    • Membrane type 1 metalloprotease antibody
    • Membrane type matrix metalloproteinase 1 antibody
    • Membrane-type matrix metalloproteinase 1 antibody
    • Membrane-type-1 matrix metalloproteinase antibody
    • MMP 14 antibody
    • MMP X1 antibody
    • MMP-14 antibody
    • MMP-X1 antibody
    • Mmp14 antibody
    • MMP14_HUMAN antibody
    • MMPX1 antibody
    • MT MMP 1 antibody
    • MT-MMP 1 antibody
    • MT1 MMP antibody
    • MT1-MMP antibody
    • MT1MMP antibody
    • MTMMP 1 antibody
    • MTMMP1 antibody
    see all

References

This product has been referenced in:
  • Swayampakula M  et al. The interactome of metabolic enzyme carbonic anhydrase IX reveals novel roles in tumor cell migration and invadopodia/MMP14-mediated invasion. Oncogene 36:6244-6261 (2017). Read more (PubMed: 28692057) »
  • Yang H  et al. Knockdown of RHOC by shRNA suppresses invasion and migration of cholangiocellular carcinoma cells via inhibition of MMP2, MMP3, MMP9 and epithelial-mesenchymal transition. Mol Med Rep 13:5255-61 (2016). Read more (PubMed: 27108649) »
See all 9 Publications for this product

Customer reviews and Q&As

Question
Answer

Thank you for contacting us. The paper that first describes the inhibition of MMP14 activity by this clone is the Galvez 2001 reference listed towards the bottom of the online datasheet, in figure 5. It also describes production of the clone and others that inhibit activity: Gálvez BG et al. Membrane type 1-matrix metalloproteinase is activated during migration of human endothelial cells and modulates endothelial motility and matrix remodeling. J Biol Chem 276:37491-500 (2001). PubMed: 11448964 Click here (or use the following: https://www.abcam.com/index.html?section=western&pageconfig=technical&intAbID=78738&mode=questionaire). Here is a link to the PDF file: http://www.jbc.org/content/276/40/37491.full.pdf I hope this information is helpful to you. Please do not hesitate to contact us if you need any more advice or information.

Read More

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

Sign up