|Detection of Mouse/Rat SODD/BAG4 by Western Blot. Western blot shows lysates of A20 mouse B cell lymphoma cell line, CH‑1 mouse B cell lymphoma cell line, and NRK rat normal kidney cell line. PVDF membrane was probed with 1 µg/mL of Mouse/Rat SODD/BAG4 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4349) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). Specific bands were detected for SODD/BAG4 at approximately 65 - 70 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.|
Tumor necrosis factor receptor-1 (TNF-R1) and other TNF receptor superfamily members, such as DR3, contain intracellular death domains (DD) and are capable of initiating apoptosis when activated by their ligands. Silencer of Death Domains (SODD) was identified as being involved in the cellular mechanism to protect against ligand-independent signaling by TNF-R1 and other DD receptors. SODD, also known as Bcl-2-Associated Athanogene 4 (BAG4), is a 457 amino acid (aa), anti‑apoptotic protein that functions through interactions with a variety of proteins including BCL-2, Raf-protein kinase, steroid hormone receptors, growth factor receptors, and members of the heat shock protein 70 kDa family. SODD is a ubiquitously expressed, cytoplasmic protein that contains a C terminal BAG domain that can bind and inhibit the chaperone activity of Hsc70/Hsp70. The association of SODD with the DD of TNF-R1 prevents constitutive activation of the TNF-R1 signaling pathway. Binding of TNF to TNF-R1 releases SODD and permits adapter molecules such as TRADD to associate with TNF-R1 leading to the activation of TNF signaling pathways such as apoptosis and NF kappa B activation.