Cell Signaling Technology

Product Pathways - Tyrosine Kinase/ Adaptors

14-3-3 β/α Antibody #9636

Applications Reactivity MW (kDa) Source
W H M R Mk 28 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

14-3-3 β/α Antibody detects endogenous levels of total 14-3-3 β/α protein.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) derived from the sequence of human 14-3-3 β/α. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa, NIH/3T3, C6 and COS cells, using 14-3-3 β/α Antibody.

Background

The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways (1,2). 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ and η that have been identified in mammals. The initially described α and δ isoforms are confirmed to be phosphorylated forms of β and ζ, respectively (3). Through their amino-terminal α helical region, 14-3-3 proteins forms homo- or heterodimers that interact with a wide variety of proteins: transcription factors, metabolic enzymes, cytoskeletal proteins, kinases, phosphatases and other signaling molecules (3,4). The interaction of 14-3-3 proteins with their targets is primarily through a phospho-Ser/Thr motif. However, binding to divergent phospho-Ser/Thr motifs, as well as phosphorylation independent interactions has been observed (4). 14-3-3 binding masks specific sequences of the target protein, and therefore, modulates target protein localization, phosphorylation state, stability and molecular interactions (1-4). 14-3-3 proteins may also induce target protein conformational changes which modify target protein function (4,5). Distinct temporal and spatial expression patterns of 14-3-3 isoforms have been observed in development and in acute response to extracellular signals and drugs, suggesting that 14-3-3 isoforms may perform different functions despite their sequence similarities (4). Several studies suggest that 14-3-3 isoforms are differentially regulated in cancer and neurological syndromes (2,3).

  1. Muslin, A.J. and Xing, H. (2000) Cell Signal 12, 703-9.
  2. Mackintosh, C. (2004) Biochem. J. 381, 329-42.
  3. Dougherty, M.K. and Morrison, D.K. (2004) J. Cell Sci. 117, 1875-84.
  4. Yaffe, M.B. (2002) FEBS Lett. 513, 53-7.
  5. Bridges, D. and Moorhead, G.B. (2004) Sci. STKE 2004, re10.

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

Product Pathways

Drug Discovery Tools

Featured Technologies

Protein Classes