Product Pathways - Apoptosis / Autophagy
Bmf Antibody #4692
| Applications | Reactivity | MW (kDa) | Source |
|---|---|---|---|
| W | H M R Mk | 18 | Rabbit |
Applications Key:
W=Western Blotting
Reactivity Key:
H=Human
M=Mouse
R=Rat
Mk=Monkey
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
Bmf Antibody detects endogenous levels of Bmf protein. It does not cross-react with other Bcl-2 family members at endogenous levels.
Source / Purification
Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to residues in the amino-terminus of Bmf. Antibodies are purified by protein A and peptide affinity chromatography.
Western Blotting
Western blot analysis of extracts from Jurkat (human), C6 (rat), and NIH/3T3 (mouse) cells, using Bmf Antibody.
Background
The -BH3-only+ proteins are a group of pro-apoptotic proteins of the Bcl-2 family that share the conserved BH3 domain but lack BH1, BH2, and BH4 (1). This short BH3 domain is essential for interaction with pro-survival members of the Bcl-2 family and allows for their pro-apoptotic activity. A large number of -BH3-only+ proteins have been identified in mammals, including Bmf, Bad, Bik, Bid, Bim, Hrk, Noxa, and Puma. Many of these proteins appear to display distinct roles in apoptosis through tissue-specific expression. Bmf (Bcl-2-modifiying factor) was originally identified in a yeast two-hybrid screen using the pro-survival protein Mcl-1 as bait (2). Bmf appears to be widely expressed, with bmf mRNA observed in cell lines of B- and T-lymphoid, myeloid, or fibroblastoid origin and in mouse embryos at all developmental stages. Bmf protein is seen most abundantly in pancreas, liver, kidney, and hematopoietic tissues (2, 3). Bmf interacts with several pro-survival Bcl-2 proteins including Mcl-1, Bcl-2, Bcl-xL, and Bcl-w, and that interaction depends on the BH3 domain (2). Like Bim, Bmf has been reported to bind to cytoskeletal structures. Bmf is normally sequestered to myosin V motors through association with dynein light chain 2 (DLC2). Certain damage signals, such as the detachment of adherent cell lines from their substratum (anoikis), triggers the release of Bmf and subsequent binding to the pro-surivival Bcl-2 proteins (2).
- Puthalakath, H. and Strasser, A. (2002) Cell Death Diff. 9, 505-512.
- Puthalakath, H. et al. (2001) Science 293, 1829-1832.
- Morales, A. A. et al. (2004) Leukemia 18, 41-47.
Application References
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