Purification notesab53127 was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/300 - 1/1000. Detects a band of approximately 116 kDa (predicted molecular weight: 116 kDa).
FunctionInvolved in calcium induced regulation of ion channel and activation of the map kinase signaling pathway. May represent an important signaling intermediate between neuropeptide activated receptors or neurotransmitters that increase calcium flux and the downstream signals that regulate neuronal activity. Interacts with the SH2 domain of Grb2. May phosphorylate the voltage-gated potassium channel protein Kv1.2. Its activation is highly correlated with the stimulation of c-Jun N-terminal kinase activity. Involved in osmotic stress-dependent SNCA 'Tyr-125' phosphorylation. In concert with SRC, plays an important role in osteoclastic bone resorption. Both the formation of a SRC-PTK2B complex, and SRC kinase activity are necessary for this function. The Tyr-402 phosphorylated form serves as a docking site for SRC and is important for the organization of the osteoclast actin cytoskeleton and attachment sites and for bone resorption.
Tissue specificityMost abundant in the brain, with highest levels in amygdala and hippocampus. Low levels in kidney. Also expressed in spleen and lymphocytes.
Sequence similaritiesBelongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily. Contains 1 FERM domain. Contains 1 protein kinase domain.
Post-translational modificationsPhosphorylated on tyrosine residues in response to various stimuli that elevate the intracellular calcium concentration, as well as by PKC activation. Recruitment by nephrocystin to cell matrix adhesions initiates Tyr-402 phosphorylation. In monocytes, adherence to substrata is required for tyrosine phosphorylation and kinase activation. Angiotensin II, thapsigargin and L-alpha-lysophosphatidic acid (LPA) also induce autophosphorylation and increase kinase activity.
Cellular localizationCytoplasm. Cell membrane. Interaction with nephrocystin induces the membrane-association of the kinase.