Technical Data
SEK1, phosphorylated (Ser257,Thr261) (MKK4, SAPK, Erk Kinase, MKK4, Jun Kinase Kinase, JNKK)
SAPK/Erk kinase (SEK1), also known as MKK4 or Jun kinase kinase (JNKK), activates the MAP kinase homologues SAPK and JNK in response to various cellular stresses and inflammatory cytokines. Activation of SEK1 occurs through phosphorylation of serine and threonine residues at positions 257 and 261, respectively, by MEKK. Like MEK, SEK is a dual-specificity protein kinase that phosphorylates SAPK/JNK at a conserved T*PY* site in its activation loop. Phosphorylation by Akt at Ser80 inhibits SEK1 and suppresses the stress-activated signal transduction.

Suitable for use in ELISA and Western Blot. Other applications not tested.

Recommended Dilutions:
Western Blot: 1:1000. Incubate membrane with diluted antibody in 5% BSA, 1X TBS, 0.1% Tween-20 at 4C with gentle shaking, overnight.
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
PabIgGAffinity Purified
100ul-20CBlue IceHumanRabbit
Not Determined
Synthetic phospho-peptide corresponding to residues surrounding Ser257/Thr261 of human SEK1, conjugated to KLH. Species Sequence Homology: Xenopus and Zebra fish.
Purified by Protein A and peptide affinity chromatography.
Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol
Recognizes endogenous levels of human SEK1/MKK4 only when phosphorylated at serine 257 and threonine 261. Does not crossreact with the corresponding phosphorylated residues of MEK1, MEK2 or MKK3. Species Crossreactivity: mouse, rat and Drosophilia.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Davis, R.J. (1994) Trends Biochem. Sci. 19, 470-473 2. Sanchez, I. et al. (1994) Nature 372, 794-798. 3. Yan, M. et al. (1994) Nature 372, 798-800. 4. Kyriakis, J.M. et al. (1994) Nature 369, 156-160. 5. Park, H. et al. (2002) J. Biol. Chem. 277, 2573-2578.