The Cleaved-CASP3 p17 (D175) Polyclonal Antibody is a highly specific antibody designed to recognize and bind the cleaved p17 subunit of Caspase-3 at the D175 site with exceptional affinity and selectivity. Caspase-3 is a key executioner caspase in the apoptosis pathway, which is activated through proteolytic cleavage of its inactive 32 kDa proenzyme into the active p17 and p12 subunits. The active form plays a central role in the cleavage of numerous substrates, leading to the morphological and biochemical hallmarks of programmed cell death. This antibody specifically recognizes the cleaved (activated) form, making it an essential tool for studying apoptotic signaling, cell death mechanisms, and related biological processes. Produced in Rabbit hosts and purified by affinity chromatography, this IgG antibody exhibits superior binding characteristics and is reactive against Human, Mouse, and Rat samples. The high purity and specificity of this reagent ensure minimal cross-reactivity and background noise, enabling researchers to obtain clear and reproducible results.
This antibody is particularly well-suited for Western Blot (WB), Immunohistochemistry (IHC), and Immunofluorescence (IF) applications. It has been validated by Western Blot analysis of various cell lysates, immunohistochemistry of paraffin-embedded human stomach cancer tissue, and immunofluorescence analysis of rat liver tissue, demonstrating consistent and reliable performance across multiple experimental platforms. Supplied as a kit, this product also includes Bradford Reagent for accurate total protein quantification and sample normalization. Its versatility and robust performance make it an excellent choice for both basic apoptosis research and translational studies in oncology, neurodegeneration, and developmental biology, allowing researchers to advance their understanding of Caspase-3 activation and apoptotic pathways in health and disease.