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Bcl-2 is considered to be novel among proto-oncogenes because it blocks apoptosis (programmed cell death) in many cell types. Apoptosis is an active form of cellular suicide that typically requires new RNA and protein synthesis and is associated with distinct morphological changes including cell shrinkage, cytoplasm membrane blebbing, nuclear fragmentation and DNA degradation. Because Bcl-2 blocks apoptosis it may contribute to tumorigenisis by prolonging cell survival, rather than by accelerating the rate of cell proliferation. Human Bcl-2 protein migrates at a molecular weight of ∽26 kDa by SDS-PAGE. Bcl-2/100 recognizes a 26 kDa band representing human Bcl-2. Additional minor bands at 27-31 kDa and 18-21 kDa may also be visualized. The 27-31 kDa upper band may represent a larger isoform, whereas the 18-21 kDa lower band may be an internal translation or proteolytic product, therefore, a synthetic peptide corresponding to amino acids 41-54 (GAAPAPGIFSSQPG) of human Bcl-2 was used as immunogen. This peptide sequence is not conserved between human and mouse. Bcl-2/100 does not cross-react with mouse Bcl-2. For detection of mouse Bcl-2 refer to clone 3F11 (Cat. No. 554218), polyclonal rabbit anti-rat/mouse Bcl-2 antiserum (Cat. No. 554087), and polyclonal rabbit anti-mouse Bcl-2 antiserum (Cat. No. 554279).
