Phospho-14-3-3 ζ/δ (Ser58)/η (Ser59)/γ (Ser59)/β/α (Ser60) (E6B3G) Rabbit mAb #52631
- WB
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 28 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Phospho-14-3-3 ζ/δ (Ser58)/η (Ser59)/γ (Ser59)/β/α (Ser60) (E6B3G) Rabbit mAb detects endogenous levels of 14-3-3 ζ/δ only when phosphorylated at Ser58, 14-3-3 η and 14-3-3 γ only when phosphorylated at Ser59, and 14-3-3 α/β only when phosphorylated at Ser60. This antibody does not cross-react with 14-3-3 ε, 14-3-3 θ, or 14-3-3 σ. This antibody also recognizes a non-specific band of unknown origin at 80 kDa and 180 kDa.
Species Reactivity:
Human, Mouse, Rat
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Monkey, Chicken, Bovine, Pig
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser58 of human 14-3-3 ζ/δ protein.
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 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).
Phosphorylation of 14-3-3ζ at Ser58 may regulate dimerization and affect its ability to interact with partner proteins, including p53 and ASK1 (6,7).
Limited Uses
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