|Detection of Human/Mouse/Rat BAK by Western Blot. Western blot shows lysates of HEK293 human embryonic kidney cell line, CH‑1 mouse B cell lymphoma cell line, and PC‑12 rat adrenal pheochromocytoma cell line. PVDF membrane was probed with 1 µg/mL of Human/Mouse/Rat BAK Antigen Affinity-purified Polyclonal Antibody (Catalog # AF8161) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for BAK at approximately 29 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.|
BAK (Bcl-2 homologous antagonist/killer; also BAK1) is a 25‑30 kDa member of the BCL-2 family of proteins. It is widely expressed, and participates in the apoptotic cycle. BAK is an outer mitochondrial membrane protein that is inactive as a Zn-dependent homodimer. Upon activation by p53 or tBID, BAK oligomerizes, creating a pore in the mitochondrial membrane and allowing for cytochrome C release. Human BAK is 211 amino acids (aa) in length and contains three BCL-2 homology domains (aa 74‑88, 117 ‑136 and 169‑184), a Zn-binding region (aa 160‑166) and a C-terminal transmembrane segment (aa 188‑205). Amino acids 67‑94 mediate oligomerization of BAK. There are two potential isoform variants; one shows an alternate start site at Met96, while a second shows a deletion of aa 46‑66. Over amino acids 20‑124, human BAK shares 76% aa identity with mouse BAK.
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