Technical Data
J2475-05B
SEK1 (MKK4, SAPK, Erk Kinase, MKK4, Jun Kinase Kinase, JNKK)
Description:
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 (1-3). 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 (4). Phosphorylation by Akt at Ser80 inhibits SEK1 and suppresses the stress-activated signal transduction (5).

Applications:
Suitable for use in ELISA, Western Blot and Immunoprecipitation. Other applications not tested.

Recommended Dilution:
Western Blot: 1:1000.
Immunoprecipitation: 1:50.
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
TypeIsotypeCloneGrade
PabIgGAffinity Purified
SizeStorageShippingSourceHost
100ul4C (-20C Glycerol)Blue IceHumanRabbit
Concentration:
Not determined
Immunogen:
Synthetic peptide corresponding to residues surrounding the N-terminus of human SEK1/MKK4 (KLH).
Purity:
Purified by protein A and peptide affinity chromatography.
Form
Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol.
Specificity:
Recognizes total levels of endogenous human SEK1/MKK4 at 44kD. Species Crossreactivity: mouse, rat and monkey. Does not cross-react with MEK1, MEK2 or MKK3. MW: 44kD.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Davis, R.J. (1994) Trends Biochem. Sci. 19, 470473. 2. Sanchez, I. et al. (1994) Nature 372, 794798. 3. Yan, M. et al. (1994) Nature 372, 798800. 4. Kyriakis, J.M. et al. (1994) Nature 369, 156160. 5. Park, H. et al. (2002) J. Biol. Chem. 277, 25732578.