Antigen-Affinity Purified MARCKS (Phospho-Ser152/156) Polyclonal Antibody

Background
Myristoylated Alanine-Rich C Kinase Substrate (MARCKS) is a major substrate for phosphorylation by protein kinase C (PKC). The phosphorylation of Ser152/156 can be used as a measure of PKC activation. Moreover, MARCKS is a member of a family of calmodulin binding proteins. Phosphorylation of Ser152/156 modulates the binding of MARCKS to calmodulin.

Antigen
This antibody was developed against synthetic phosphopeptide corresponding to amino acids residues surrounding the phospho-Ser152 and phospho-Ser156 of rat MARCKS. The antibody was purified by sequential chromatography on phospho- and non-phosphopeptide affinity columns.

Application Notes
An ~87 kDa band is observed in rat brain homogenate. Immunolabeling is blocked by the Ser152/156 phosphopeptide but not by the non-phosphopeptide. Human, mouse, rat, and Xenopus have 100% amino acid sequence identity with the antigen used to raise the antibody. Antibody dilutions and tissue load should be based on tissue type and expected phosphorylation state expected expression level.

Genebank Info (Protein)
NP_002347

Reference
1. Palmer, R.H., Schönwasser, D.C., Rahman, D., Pappin, D.J.C., Herget, T., and Parker, P.J., FEBS Letters, 378 (1996) 281 - 285.
2. Spizz, G. and Blackshear, P.J., J. Biol. Chem., 271 (1996) 553 - 562.
3. Thelen, M., Rosen, A., Nairn, A.C., and Aderem, A.,  Nature (London), 351 (1991) 320 - 322.
4. Hartwig, J.H., Thelen, M., Rosen, A., Janmey, P.A., Nairn, A.C., and Aderem, A., Nature (London), 356 (1992) 618 - 622.
5. McGlade-Mcculloh, E., Yamamoto, H., Tan, S.-E., Brickey, D.A. and Soderling, T.R. Nature (London) 362 (1993) 640 - 642.