Matrix metalloproteinases (MMPs) or gelatinases play an important role in the early invasion of malignant tumors. These enzymes may be released directly from tumor cells, or may be derived from fibroblasts that have been stimulated with the extracellular MMP-inducer EMMPRIN. Studies have demonstrated that EMMPRIN stimulates human fibroblast production of interstitial collagenase, stromelysin-1, and gelatinase A (MMP-2), which is essential for tissue degradation and remodeling during tumor invasion and wound healing.

The antibody recognizes EMMPRIN.

Epitope: Unknown

Human synovial fibroblasts.

Imunohistochemistry Analysis: A 1:100 dilution from a previous lot detected EMMPRIN in human adenocarcinoma tissue.

Research Category
Cell Structure

Research Sub Category
MMPs & TIMPs

This Anti-EMMPRIN [CD147] Antibody, clone 1S9-2A is validated for use in WB, IH for the detection of EMMPRIN [CD147].

Evaluated by Western Blot in HeLa cell lysate.

Western Blot Analysis: 0.1 µg/ml of this antibody detected EMMPRIN on 10 µg of HeLa cell lysate.

~ 35-58 kDa The extent of CD147 glycosylation is tissue-specific and is responsible for a variation in the apparent molecular mass from 35 kDa to 58 kDa

Format: Purified

Protein G Purified

Purified mouse monoclonal IgG2aκ in buffer containing 0.1 M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.

Control
HeLa cell lysate

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

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.