Product Pathways - Tyrosine Kinase / Adaptors
14-3-3 ε Antibody #9635
|W||H M R Mk||Endogenous||28||Rabbit|
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.
Specificity / Sensitivity
14-3-3 ε Antibody detects endogenous levels of total 14-3-3 ε protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the sequence of human 14-3-3 ε. Antibodies are purified by protein A and peptide affinity chromatography.
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 form 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 that 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).
- Muslin, A.J. and Xing, H. (2000) Cell Signal 12, 703-9.
- Mackintosh, C. (2004) Biochem J 381, 329-42.
- Dougherty, M.K. and Morrison, D.K. (2004) J Cell Sci 117, 1875-84.
- Yaffe, M.B. (2002) FEBS Lett 513, 53-7.
- Bridges, D. and Moorhead, G.B. (2004) Sci STKE 2004, re10.
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For Research Use Only. Not For Use In Diagnostic Procedures.