Cell Signaling Technology

Product Pathways - Stem Cell and Lineage Markers

GFI1b (D3G2) Rabbit mAb #5849

Applications Reactivity Sensitivity MW (kDa) Isotype
W H M R Mk Endogenous 35, 42 Rabbit IgG

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

Protocols

Specificity / Sensitivity

GFI1b (D3G2) Rabbit mAb recognizes endogenous levels of total GFI1b protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human GFI1b protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using GFI1b (D3G2) Rabbit mAb.

Background

GFI1b and its homolog GFI1 are transcriptional repressors and important regulators of erythroid and megakaryocytic development and differentiation (1,2). GFI1b negatively regulates transcription by recruiting chromatin regulatory proteins including CoREST, the histone demethylase LSD1 and HDACs 1 and 2, which associate with GFI1b via its SNAG repression domain (3). GFI1b has also been shown to control the differentiation of erythroid and megakaryocytic progenitors by regulating TGF-β signaling at the bipotent progenitor stage (4). Inactivation of GFI1b in mice leads to embryonic lethality due to failure to produce functional erythrocytes and megakaryocytes (2). The GFI1b gene locus can be autoregulated by binding to its own promoter in hematopoietic cells, likely through interacting with GATA-1, another transcription factor essential for erythroid and megakaryocytic development (5). Mutations in GFI1b are implicated in various leukemias (6) and GFI1b has been found in a complex with GATA-1 and SUZ12 on repressed genes in erythroleukemia cells (7).

  1. Duan, Z. and Horwitz, M. (2003) Hematology 8, 339-44.
  2. Saleque, S. et al. (2002) Genes Dev 16, 301-6.
  3. Saleque, S. et al. (2007) Mol Cell 27, 562-72.
  4. Randrianarison-Huetz, V. et al. (2010) Blood 115, 2784-95.
  5. Vaziri, K. et al. (2005) South Med J 98, 825-6.
  6. Elmaagacli, A.H. et al. (2007) Br J Haematol 136, 212-9.
  7. Yu, M. et al. (2009) Mol Cell 36, 682-95.

Application References

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

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