Anti-Cleaved-ADAM17 (R215) Antibody

Raised in rabbit and affinity-purified as a polyclonal reagent, this unconjugated primary antibody from Antibodies.com selectively binds the cleaved, activated form of ADAM17 (also known as TACE, tumor necrosis factor-α-converting enzyme) at the R215 neo-epitope. ADAM17 is a membrane-anchored metalloprotease and sheddase responsible for releasing soluble TNF-α, several EGFR ligands (TGF-α, amphiregulin, HB-EGF), and numerous other type I and type II transmembrane substrates involved in inflammation, growth factor signaling, and disease contexts ranging from cancer to neurodegeneration. By recognizing only the R215-cleaved species rather than the full-length zymogen, the antibody enables researchers to specifically monitor proteolytic activation of ADAM17 in cell lysates and tissue homogenates.

Validated for Western blot across human, mouse, and rat samples, the reagent is supplied as 100 µl of a 1 mg/ml stock in PBS containing 0.1% sodium azide and 50% glycerol, ready to dilute into standard blocking buffer for chemiluminescent or fluorescent detection. Polyclonal rabbit antibodies are particularly useful when probing conformational or processing-dependent epitopes, and the unconjugated format gives laboratories full flexibility over secondary antibody choice, detection chemistry, and multiplexing strategies. The 50% glycerol cryoprotectant allows the stock to be kept at –20 °C without freeze-thaw damage of the working vial, and preparing single-use aliquots is recommended to limit repeated freeze-thaw cycles during long-term studies.

This reagent is intended for research use only and is appropriate for investigations of ectodomain shedding, receptor-ligand signaling, inflammation, and metalloprotease biology, where distinguishing inactive pro-ADAM17 from its cleaved, catalytically competent form is essential to correctly interpret downstream release of TNF-α and EGFR-family ligands.