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Western blot of 10 µg of rat brain lysate showing specific immunolabeling of the ~87 kDa MARCKS protein phosphorylated at Ser152/156 Lane 1). Immunolabeling is blocked by the Ser152/156 phosphopeptide used as antigen (Lane 2). The corresponding dephosphopeptide did not block the immunolabeling (not shown).
|Tested species reactivity||Rat|
|Published species reactivity||Mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser152/156 of rat MARCKS conjugated to KLH|
|Storage buffer||0.01M HEPES, pH 7.5, with 0.15M NaCl, 100µg/ml BSA, 50% glycerol|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Western Blot (WB)||See 1 publications below|
This antibody is predicted to react with bovine, chicken, human, mouse, Xenopus and zebrafish based on 100% sequence homology.
This antibody is specific for the ~87 kDa MARCKS protein phosphorylated at Ser152 and Ser156 in Western blots of rat brain homogenates. Immunolabeling is blocked by the phosphopeptide used as the antigen but not by the corresponding dephosphopeptide.
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 Ser152/156 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 protein and phosphorylation of Ser152/156 modulates the binding of MARCKS to calmodulin (Verghese et al., 1994).
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
ENaC activity and expression is decreased in the lungs of protein kinase C-α knockout mice.
PA1-4629 was used in western blot to study the regulation of alveolar epithelial Na(+) channels using a PKC-alpha knockout model
|Eaton AF,Yue Q,Eaton DC,Bao HF||American journal of physiology. Lung cellular and molecular physiology (307:L374)||2014|
156); 3-hydroxy-2-methylbutyryl-CoA dehydrogenase; AB-binding alcohol dehydrogenase; amyloid-beta peptide binding alcohol dehydrogenase; endoplasmic reticulum-associated amyloid beta-peptide-binding protein; hydroxysteroid (17-beta) dehydrogenase 10; hydroxysteroid dehydrogenase 10; mitochondrial ribonuclease P protein 2; mitochondrial RNase P subunit 2; phospho-Myristoylated Alanine-Rich C Kinase Substrate (Ser152; short chain dehydrogenase/reductase family 5C member 1; short chain dehydrogenase/reductase family 5C, member 1; short chain L-3-hydroxyacyl-CoA dehydrogenase type 2; short chain type dehydrogenase/reductase XH98G2
17b-HSD10; ABAD; CAMR; DUPXp11.22; ERAB; HADH2; HCD2; HSD17B10; MHBD; MRPP2; MRX17; MRX31; MRXS10; SCHAD; SDR5C1; XH98G2