epitope corresponding to phosphorylated Ser 159 of MARCKS of human origin
Modification
Phosphoralated
Modification Notes
Myristolated Alanine-Rich C-Kinase Substrate (MARCKS) is a major in vivo substrate of protein kinase C (PKC) and for the lipid-activated PKC-related kinase (PRK1) (1). Furthermore, PRK1 and PKC phosphorylate MARCKS on the same sites in vitro, serine 152, 156 and 163. MARCKS serves as an in vitro substrate for PKC m as well. However, in contrast to other PKCs, MARCKS is phosphorylated by PKC m only at serine 156 and not at serines 152 and 163, implicating a differential regulation by PKC m. Therefore, control of MARCKS phosphorylation on these previously identified 'PKC' sites may be regulated under certain circumstances by PRK as well as PKC mediated signalling pathways. MARCKS associates with the plasma membrane in response to PKC-catalyzed phosphorylation of MARCKS. It has been suggested that MARCKS is capable of associating with the plasma membrane through binding to phospholipids without interaction with membranous proteins.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIP
recommended for detection of Ser 159/ phosphorylated MARCKS of mouse, rat and human origin by WB and IP:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to phosphorylated Ser 159 of MARCKS of human origin
Tissue Specificity
epitope corresponding to phosphorylated Ser 159 of MARCKS of human origin