Technical Data

J2475-05C
Clone Type
Polyclonal
Host
Rabbit
Source
Human
Isotype
IgG
Grade
Affinity Purified
Applications
IP WB
Crossreactivity
Hu
Gene ID
6416
Shipping Temp
Blue Ice
Storage Temp
-20°C
Rabbit Anti-SEK1, phosphorylated (Ser80) (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 (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 serine 80 inhibits SEK1 and suppresses the stress-activated signal transduction (5).

Applications
Suitable for use in Western Blot, Immunoprecipitation. Other applications not tested.
Recommended Dilution
Western Blot: 1:1000 Immunoprecipitation 1:25 Optimal dilutions to be determined by the researcher.
Storage and Stability
May be stored at 4°C for short-term only. For long-term storage, store at -20°C. Aliquots are stable for at least 12 months at -20°C. 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.
Immunogen
Synthetic phosphopeptide (KLH coupled) corresponding to residues surrounding Ser80 of human SEK1/MKK4.
Form
Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, BSA, 50% glycerol.
Purity
Purified by protein A and peptide affinity chromatography.
Specificity
Detects endogenous levels of SEK1/MKK4 only when phosphorylated at serine 80. Does not crossreact with the corresponding phosphorylated residues of MEK1, MEK2 or MKK3.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.

References
(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.
USBio References
No references available
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