Cell Signaling Technology

Product Pathways - Apoptosis

Bmf (G81) Antibody #5889

Applications Reactivity Sensitivity MW (kDa) Source
W H (M) (R) Endogenous 21 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Bmf (G81) Antibody recognizes endogenous levels of total Bmf protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly81 of human Bmf protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from RPMI 8226 and Ramos cells using Bmf (G81) Antibody.

Western Blotting

Western Blotting

Western blot analysis of extracts from 293T cells, mock transfected (-) or transfected with Myc/Flag-tagged Bmf (+), using Bmf (G81) 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 the 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).

  1. Puthalakath, H. and Strasser, A. (2002) Cell Death Diff. 9, 505-512.
  2. Puthalakath, H. et al. (2001) Science 293, 1829-1832.
  3. Morales, A. A. et al. (2004) Leukemia 18, 41-47.

Application References

Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!

Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

Products