Product Pathways - Transcription Factors
FoxK1 Antibody #12025
|12025S||100 µl (10 western blots)||---||In Stock||---|
|12025||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Monkey||Endogenous||97||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Specificity / Sensitivity
FoxK1 Antibody recognizes endogenous levels of total FoxK1 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg692 of mouse FoxK1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors defined by the presence of a winged helix DNA binding domain called a Forkhead box (1). In humans, there are over 40 known Fox protein family members, divided into 19 subfamilies, which have evolved to regulate gene transcription in diverse and highly specialized biological contexts throughout development (2). Mutations that disrupt the expression of Fox gene family members have consequently been implicated in a broad array of human disorders, including immunological dysfunction, infertility, speech/language disorders, and cancer (3,4).
FoxK1 belongs to a subfamily of Fox proteins along with FoxK2. FoxK1 functions as a transcriptional repressor of downstream target genes including FoxO4, Mef2, P21, PPGB, and SM α-actin (5-7). There are two isoforms of FoxK1: FoxK1-α and FoxK1-β. The β isoform has a truncated C terminus compared to the α isoform. The two isoforms of FoxK1 show reciprocal expression patterns during muscle regeneration. FoxK1-β is expressed mainly in quiescent satellite cells (8), whereas FoxK1-α is the dominant isoform in proliferating myoblasts from activated satellite cells (9). Both isoforms of FoxK1 jointly regulate proliferation and differentiation of myogenic stem cells during development and muscle regeneration (10).
- Myatt, S.S. and Lam, E.W. (2007) Nat Rev Cancer 7, 847-59.
- Jackson, B.C. et al. (2010) Hum Genomics 4, 345-52.
- Hannenhalli, S. and Kaestner, K.H. (2009) Nat Rev Genet 10, 233-40.
- Benayoun, B.A. et al. (2011) Trends Genet 10, 224-32.
- Hawke, T.J. et al. (2003) J Biol Chem 278, 4015-20.
- Freddie, C.T. et al. (2007) Nucleic Acids Res 35, 5203-12.
- Shi, X. et al. (2012) J Cell Sci , .
- Garry, D.J. et al. (1997) Dev Biol 188, 280-94.
- Yang, Q. et al. (1997) Mol Cell Biol 17, 5236-43.
- Garry, D.J. et al. (2000) Proc Natl Acad Sci U S A 97, 5416-21.
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