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The bcl-2 gene was first discovered in t(14:18) follicular lymphomas. Translocation of bcl-2 sequences from chromosome 18 onto the transcriptionally active immunoglobulin locus at chromosome band 14q32 in B-cells deregulates bcl-2 gene expression, resulting in high levels of bcl-2 mRNA. Bcl-2 protein blocks apoptosis (programmed cell death), and thereby may contribute to tomorigenesis by prolonging cell survival rather than by accelerating the rate of cell proliferation. Abundant evidence implicates this protein in the suppression of apoptosis in many types of cells. Bcl-2 is an intracellular membrane protein and resides primarily in the nuclear envelope, outer mitochondrial membrane and endoplasmic reticulum. The reduced molecular weight of Bcl-2 is 26 kDa. parClone 4D7 recognizes human Bcl-2. A synthetic peptide containing amino acids 61-76 of the human Bcl-2 protein was used as immunogen. This peptide sequence differs from that of mouse Bcl-2 and hence 4D7 does not cross-react with mouse. 4D7 recognizes Bcl-2 as a 26 kDa band; however, additional higher molecular weight bands have been observed in some cell types. These bands may represent oligomers of Bcl-2, which have been reported to occur with members of the Bcl-2 family during the preparation of nonionic detergent extracts.
