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Apoptosis, the best-characterized form of programmed cell death, is essential for normal animal development, tissue homeostasis, and disease. We offer many primary antibodies for studying various targets along the apoptosis pathway. Whether your research is focused on apoptosis markers, apoptotic morphological changes, or the biochemical features of apoptosis, we have a broad selection of antibodies for your needs. Invitrogen apoptosis antibodies are designed to dependably detect the key apoptosis targets. Each antibody is validated* for use in various applications. To learn more about apoptosis, visit the Antibody Learning Center’s Overview of Apoptosis article.
There are a wide variety of Invitrogen antibodies for each step of the apoptosis pathways. Provided in the table below are common targets used to study apoptosis. Click on each target to see our selection of available antibodies.
Each Invitrogen apoptosis antibody is verified for use in applications such as ELISA, western blot, flow cytometry, immunofluorescence, immunohistochemistry, immunocytochemistry, and immunoprecipitation.
Figure 1. Caspase 8 Antibody in western blot. Western blot analysis of Caspase 8 was performed by loading 30 µg of HeLa WT untreated (Lane 1), HeLa WT Staurosporine treated (Lane 2), HeLa Cas9 untreated (Lane 3), HeLa Cas9 Staurosporine treated (Lane 4), HeLa Cas8 knockout untreated (Lane 5) and HeLa Cas8 knockout Staurosporine treated (Lane 6) whole cell lysate. The blot was probed with Caspase 8 Monoclonal Antibody (B.925.8) (Cat. No. MA5-15226, 1:500 dilution) and Goat anti-Mouse IgG (H+L) Superclonal Secondary Antibody, HRP conjugate (Cat. No. A28177, 0.25 µg/ml 1:4,000 dilution). Loss of signal upon CRISPR mediated knockout (KO) confirms that this antibody is specific to Caspase 8.
Figure 2. Caspase 3 Antibody in western blot. Altered expression of proteins upon cell treatment demonstrates antibody specificity. Western blot of Caspase 3 using Caspase 3 Monoclonal Antibody (3CSP01 (7.1.44)) (Cat. No. MA5-11516), shows expression of cleaved Caspase 3 upon treatment of SH-SY5Y and Jurkat cells with Etoposide and Staurosporine, respectively.
Figure 3. PARP1 (cleaved Asp214) Antibody in Flow. Jurkat cells were left unstimulated (left) or stimulated for 20 hours with CD95 (APO-1/Fas) Monoclonal Antibody (EOS9.1), Function Grade (Cat. No. 16-0958-81) coated at 5 µg/mL in a 24-well culture plate (right). The stimulated cells were then harvested and stained sequentially with Fixable Viability Dye eFluor 780 (Cat. No. 65-0865-14) and the Annexin V Apoptosis Detection Kit eFluor 450 (Cat. No. 88-8006-72), then fixed and permeabilized with the Foxp3/Transcription Factor Staining Buffer Set (Cat. No. 00-5523-00) and stained with PARP1 (cleaved Asp214) Monoclonal Antibody (HLNC4), PE (Cat. No. 12-6668-42). Total viable cells (Fixable Viability Dye eFluor 780 negative) were used for analysis.
For Research Use Only. Not for use in diagnostic procedures.
For Research Use Only. Not for use in diagnostic procedures.