Our Anti-MARCKS (Ser152,156) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects mouse and rat MARCKS (Ser152,156) and is antigen affinity purified from pooled serum. It is great for use in WB.
Western blot of rat brain lysate showing specific immunolabeling of the ~87 kDa MARCKS protein phosphorylated at Ser152,156, in the first lane (-). Phosphospecificity is shown in the second lane (+) where immunolabeling is completely eliminated by blot treatment with lambda phosphatase (λ-Ptase, 1200 units for 30 min).
Anti-MARCKS (Ser152,156) Antibody
Myristoylated Alanine-Rich C Kinase Substrate (MARCKS) is a major substrate for phosphorylation by protein kinase C (PKC) (Ouimet et al., 1990). The phosphorylation of Ser-152/156 can be used as a measure of PKC activation although these sites are also phosphorylated by PRK1 (Palmer et al., 1996) MARCKS is a member of a family of calmodulin binding proteins and phosphorylation of Ser-152/156 modulates the binding of MARCKS to calmodulin (Verghese et al., 1994)
Antigen Affinity Purified from Pooled Serum
Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser152/156 of rat MARCKS, conjugated to keyhole limpet hemocyanin (KLH).
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Prepared from pooled rabbit serum by affinity purification via sequential chromatography on phospho and non-phosphopeptide affinity columns.
10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol.
Specific for endogenous levels of the ~87 kDa MARCKS protein phosphorylated at Ser152 and Ser156. Immunolabeling is completely eliminated by treatment with λ-phosphatase.
Western blots performed on each lot.
For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
After date of receipt, stable for at least 1 year at -20°C.
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Betti, M., et al. 2011. Maternal dietary loads of α-tocopherol depress protein kinase C signaling and synaptic plasticity in rat postnatal developing hippocampus and promote permanent deficits in adult offspring. The Journal of Nutritional Biochemistry, 22(1), pp.60-70.
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