Mouse, Human Predicted to work with:
Synthetic peptide within Human PYK2 (phospho Y579) conjugated to Keyhole Limpet Haemocyanin (KLH). The exact sequence is proprietary. Peptide sequence is around the phosphorylation site of tyrosine 579(E-D-Y(p)-Y-K). Database link: Q14289
Human brain tissue; extracts from 3T3 and HepG2 cells.
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Involved 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.
Most abundant in the brain, with highest levels in amygdala and hippocampus. Low levels in kidney. Also expressed in spleen and lymphocytes.
Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily. Contains 1 FERM domain. Contains 1 protein kinase domain.
Phosphorylated 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.
Cytoplasm. Cell membrane. Interaction with nephrocystin induces the membrane-association of the kinase.
Immunohistochemical analysis of formalin-fixed, paraffin-embedded Human brain tissue sections labeling PYK2 (phospho Y579) with ab193674 at a 1/50 dilution. Right image was preincubated with blocking peptide.