Analysis Note

ControlPOSITIVE CONTROL: Bladder, breast, and ovarian carcinomas.

Application

This Anti-MMP-7 Antibody, clone ID-2 is validated for use in IF, IH, IH(P) for the detection of MMP-7.

Research CategoryCell Structure

Immunofluorescence

Immunohistochemistry on frozen and formalin-fixed paraffin embedded tissue sections: 1:100-1:200 for 60 minutes at room temperature*.

*No pretreatment /antigen retrieval required for staining routine formalin-fixed, paraffin embedded sections.

Optimal working dilutions must be determined by end user.

Research Sub CategoryMMPs & TIMPs

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

General description

Matrix metalloproteinases (MMPs) are a family of enzymes that are responsible for the degradation of extracellular matrix components such as collagen, laminin and proteoglycans. In addition to sequence homology, all MMPs share the following characteristics: the catalytic mechanism is dependent upon a zinc ion at the active center, they cleave one or more extracellular matrix components, they are secreted as zymogens which are activated by removal of an approximately 10 kDa segment from the N-terminus and they are inhibited by tissue inhibitor of metalloproteinases (TIMP). These enzymes are involved in normal physiological processes such as embryogenesis and tissue remodeling and may play an important role in angiogenesis, arthritis, periodontitis, and metastasis. Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials (e.g., 4-aminophenylmercuric acetate, APMA) and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, pancreatic carcinomas and approximately 50% of gliomas.

Immunogen

Recombinant human matrilysin.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Physical form

Purified from ascites fluid by Protein A chromatography. Liquid in 10 mM PBS, pH 7.4, with 0.2% BSA and 15 mM sodium azide.

Format: Purified

Specificity

Antibody recognizes proteins of ~28 kDa and ~18 kDa which are identified as pro (latent) and active forms of matrix metalloproteinase-7. The antibody shows no cross-reaction with the pro and active forms of other MMPs.

Cellular Localization: Cytoplasmic (Visscher et al., 1994).

Storage and Stability

Maintain at 2-8°C in undiluted aliquots for up to 12 months from date of receipt.