protein

14-3-3 epsilon Protein, Mouse (His)

HY-P75549

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

45;75;200;340;950;1600 USD

14-3-3 epsilon Protein, Mouse (His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

45;75;200;340;950;1600 USD

14-3-3 epsilon proteins are adapter proteins in various signaling pathways that bind to phosphoserine or phosphothreonine motifs to regulate chaperone activity.It positively regulates HSF1 nuclear export to the cytoplasm, forming homo- and heterodimers with YWHAZ.14-3-3 epsilon Protein, Mouse (His) is the recombinant mouse-derived 14-3-3 epsilon protein, expressed by E.coli , with N-6*His labeled tag.

Mouse

The 14-3-3 epsilon protein serves as an adapter implicated in the regulation of a diverse array of both general and specialized signaling pathways, binding to numerous partners through the recognition of phosphoserine or phosphothreonine motifs, thereby modulating the activity of the binding partner. Notably, it positively regulates the nuclear export of phosphorylated protein HSF1 to the cytoplasm. Existing as a homodimer, it also forms heterodimers with YWHAZ and interacts with various proteins, including PKA-phosphorylated AANAT, ABL1 in its phosphorylated form, ARHGEF28, BEX3, CDKN1B, the 'Thr-369' phosphorylated form of DAPK2, DENND1A, GAB2, phosphorylated GRB10, KSR1, NDEL1, PI4KB, TBC1D22A, TBC1D22B, the phosphorylated form of SRPK2, TIAM2, the 'Ser-1134' and 'Ser-1161' phosphorylated form of SOS1, ZFP36, SLITRK1, HSF1 in its phosphorylated form, RIPOR2, KLHL22, CRTC1, CRTC2 (probably when phosphorylated at 'Ser-171'), CRTC3 (probably when phosphorylated at 'Ser-162' and/or 'Ser-273'), ATP2B1, ATP2B3, and MEFV. These interactions highlight the multifaceted role of 14-3-3 epsilon in orchestrating various cellular processes and signaling events.

14-3-3 protein epsilon, N-GST; YWHAE; 14-3-3E

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris-HCL, 300 mM NaCl, pH 7.4.

Room temperature in continental US; may vary elsewhere.