Cell Signaling Technology
XP Monoclonal Antibody

Product Pathways - Protein Stability

MMP-7 (D4H5) XP® Rabbit mAb #3801

Applications Reactivity Sensitivity MW (kDa) Isotype
W IHC-P M R Endogenous 28, 20-22 Rabbit

Applications Key:  W=Western Blotting  IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key:  M=Mouse  R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

MMP-7 (D4H5) XP® Rabbit mAb detects endogenous levels of total MMP-7 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ile264 of mouse MMP-7 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts mouse intestine (MMP-7 positive), mouse colon (MMP-7 negative) and rat prostate (MMP-7 positive) tissues using MMP-7 (D4H5) XP® Rabbit mAb.

Western Blotting

Western Blotting

Western blot analysis of extracts from COS cells, untransfected or transfected with mouse MMP-7, using MMP-7 (D4H5) XP® Rabbit mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded mouse small intestine (positive, left) and mouse colon (negative, right) using MMP-7 (D4H5) XP® Rabbit mAb.


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, MMP-2, MMP-3, MMP-7 and MMP-9 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


For Research Use Only. Not For Use In Diagnostic Procedures.

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