|Detection of Human BAK by Western Blot. Western blot shows lysates of THP‑1 human acute monocytic leukemia cell line and HEK293 human embryonic kidney cell line. PVDF membrane was probed with 1-4 µg/mL of Human BAK Antigen Affinity-purified Polyclonal Antibody (Catalog # AF816) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). A specific band was detected for BAK at approximately 26 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 53-72, human BAK shares 55% aa identity with mouse BAK.
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