Anti-phospho-Myristoylated Alanine-Rich Protein Kinase C Substrate (pSer^152/156) antibody produced in rabbit

A working dilution of 1:1000 is recommended for detection of MARCKS, phosphorylated at Ser^152/156, by immunoblotting in rat hippocampal tissue homogenates.

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The proteins of myristoylated alanine-rich C kinase substrate (MARCKS) family are identified as the ubiquitous substrates of Protein Kinase C (PKC). There are two identified members of MARCKS family, a 32 kDa ubiquitously expressed protein and a 20 kDa protein that is expressed in brain, macrophages and reproductive tissues. MARCKS proteins have vital role to play in the development of brain, cellular migration and adhesion, phagocytosis, neurosecretion and postnatal survival. MARCKS is also a key regulator in the mucin granule release and thereby secretion of mucus in airway. The phosphorylation domain of MARCKS protein contains the serine residues (serine 152, 156 and 163) that are activated by PKC. Besides PKC, MARCKS is also a target for calcium-calmodulin (CaM) and is reported as the potential protein that mediates a crosstalk between CaM and PKC. MARCKS participates in regulation of cytoskeleton by binding with actin and cell membrane
Anti-phospho-MARCKS (pSer^152/156) specifically recognizes MARCKS (80 kDa) phosphorylated at serine 152/156.

synthetic phosphorylated peptide derived from the region of rat MARCKS, which is phosphorylated on serine 152/156.

Solution in 10 mM HEPES, pH 7.5, containing 150 mM NaCl, 100 μg/ml BSA and 50% glycerol.