New England Biolabs Canada
 
XP Monoclonal Antibody

Product Pathways - Angiogenesis

MMP-7 (D4H5) XP® Rabbit mAb #3801

Item# Description List Price Web Price Qty
3801S MMP-7 (D4H5) XP® Rabbit mAb - 100 µl $410.00
$369.00
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3801T MMP-7 (D4H5) XP® Rabbit mAb - 20 µl $171.00
$153.90
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*On-line ordering is for Canadian customers only. Web pricing is applicable only to orders placed online at www.neb.ca
VIEW COMPANION PRODUCTS HIDE COMPANION PRODUCTS
Application Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W Mouse, Rat Endogenous 28, 20-22 Rabbit
IHC-P

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting, IHC-P=Immunohistochemistry (Paraffin)

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). Research studies have shown that 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, 534-40.
  2. Coussens, L.M. et al. (2002) Science 295, 2387-92.
  3. Sternlicht, M.D. et al. (1999) Cell 98, 137-46.
  4. Vu, T.H. et al. (1998) Cell 93, 411-22.
  5. Nagase, H. et al. (1990) Biochemistry 29, 5783-9.

Application References

Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!


 

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