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MAP Kinase Kinase 3,6 (MKK3,6) (Ser189/207) BioAssay(TM) Phosphorylation Detection Kit

Cat no: M2363-15A

Supplier: United States Biological
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MKK3 and MKK6 are two closely related dual specificity protein kinases that activate p38 MAP kinase (1-5). MKK3 and MKK6 both phosphorylate and activate p38 MAP kinase at its activation site Thr-Gly-Tyr. They do not phosphorylate or activate the two other MAP kinases, ERK1/2 or SAPK/JNK. Phosphorylation of p38 MAP kinase dramatically stimulates the ability of p38 MAP kinase to phosphorylate protein substrates such as ATF-2 and Elk-1. MKK3 and MKK6 kinases are activated by different forms of cellular stress and inflammatory cytokines (4,5). As for MEK1/2 and SEK, activation of MKK3 and MKK6 occurs through phosphorylation of serine and threonine residues at position Ser189 and Thr193 for MKK3 (2) and Ser207 and Thr211 for MKK6 (4,5). The MKK3/MKK6 (Ser189/207) Antibody Kit provides reagents and protocols for the rapid analysis of MKK3/MKK6 (Ser189/207) phosphorylation status. The kit includes a phospho-specific antibody that recognizes MKK3/ MKK6 only when phosphorylated at Ser189/207, a MKK3 antibody (phosphorylation-state independent), protein controls and protein markers for Western Blot and the HRP Western Detection System. Applications: Suitable for use in Western Blot, Immunoprecipitation. Other applications not tested. Recommended Dilution: Western Blot: 1:1000 Immunoprecipitation: 1:250 Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4 degrees C for short-term only. For long-term storage, store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees 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.
Catalogue number: M2363-15A
Applications: Immunoprecipitation, Western Blot
Size: 1Kit
References: 1. Banerjee, S., et., J. Virol. 76: 5937-5948 (2002). 2. DeWindt, L.j., et al., J. Biol. Chem. 275: 13571-13579 (2000). 3. Kuemmerle, J.F., et al., J. Biol. Chem. 277: 20563-20571 (2002). 4. Mita, H., et al., Mol. Cell. Biol. 22: 4544-4555 (2002). 5. Yu, L., et al., EMBO J. 21: 3749-3759 (2002). 6. Derijard, B., et al., Science 267: 682-685 (1995). 7. Raingeaud, J., et al., J. Biol. Chem. 270: 7420-7426 (1995). 8. Sluss, H.K., et al., Mol. Cell. Biol. 14: 8376-8384 (1994). 9. Raingeaud, J., et al., Mol. Cell. Biol. 16(3): 1247-1255 (1996). 10. Han, J., et al., J. Biol. Chem. 271: 2886-2891 (1996).

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