Cell Signaling Technology

Product Pathways - Protein Folding/Stability

MMP9 Antibody #3852

Applications Reactivity Sensitivity MW (kDa) Source
W IHC-P H Endogenous 84, 92 Rabbit

Applications Key:  W=Western Blotting  IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key:  H=Human
Species cross-reactivity is determined by Western blot.

Protocols

Specificity / Sensitivity

MMP9 Antibody detects full length (proenzyme, 92 kDa) and cleaved (active enzyme, 84 kDa) MMP9.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues between 107-117 of human MMP9. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of partially purified, concentrated, serum-free medium containing human MMP9, using MMP9 Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human benign meningioma, using MMP9 Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human squamous cell carcinoma of the esophagus, using MMP9 Antibody.


IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human ovarian carcinoma, using MMP9 Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma, using MMP9 Antibody in the presence of control peptide (left) or antigen-specific peptide (right).

Background

The matrix metalloproteinases (MMPs) are a family of proteases that target many extracellular proteins including other proteases, growth factors, cell surface receptors and adhesion molecules (1). Among the family members, MMP2, MMP3, MMP7 and MMP9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis and apoptosis (2-4). MMP activity correlates with cancer development (2). One mechanism of MMP regulation is transcriptional (5). Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full length protein (5).

  1. McCawley, L.J. and Matrisian, L.M. (2001) Curr. Opin. Cell Biol. 13, 534-540.
  2. Coussens, L.M. et al. (2002) Science 295, 2387-2391.
  3. Sternlicht, M.D. et al. (1999) Cell 98, 137-146.
  4. Vu, T.H. et al. (1998) Cell 93, 411-422.
  5. Nagase, H. et al. (1990) Biochemistry 29, 5783-5789.

Application References

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Companion Products

This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.

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