SpecificitySome cross-reactivity with Focal Adhesion Kinase phosphorylated at tyrosine 925 (the corresponding Grb 2 binding site) may be observed in cases where Focal Adhesion Kinase is overexpressed relative to PYK 2 in the same cell system.
Purification notesPurified from rabbit serum by epitope-specific chromatography. The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated PYK 2. The final product is generated by affinity chromatography using a PYK 2-derived peptide that is phosphorylated at tyrosine 881.
Not tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
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.
Calcium regulated non receptor proline rich tyrosine kinase antibody
Calcium-dependent tyrosine kinase antibody
Cell adhesion kinase beta antibody
EC 126.96.36.199 antibody
FADK 2 antibody
Focal adhesion kinase 2 antibody
Proline-rich tyrosine kinase 2 antibody
Protein kinase B antibody
Protein Tyrosine Kinase 2 Beta antibody
Protein-tyrosine kinase 2-beta antibody
PTK2B protein tyrosine kinase 2 beta antibody
Related adhesion focal tyrosine kinase antibody
Anti-PYK2 (phospho Y881) antibody images
Western blot - Anti-PYK2 (phospho Y881) antibody (ab4801)
Predicted band size : 116 kDa
Peptide Competition: Extracts prepared from CEF cells expressing Pyk2 and plated on fibronectin were resolved by SDS-PAGE on a 10% Tris glycine gel. The proteins were then transferred to nitrocellulose. Membranes were blocked with a 5% BSA-TBST buffer overnight at 4oC, then were incubated with 0.75 µg/mL ab4801 for two hours at room temperature in a 3% BSA-TBST buffer, following prior incubation with: no peptide (1), the peptide immunogen (2), the non-phosphopeptide corresponding to the Pyk2 phosphopeptide (3), the phosphopeptide corresponding to the tyrosine 861 of the FAK protein (4), and a generic phosphotyrosine peptide (5). After washing, membranes were incubated with goat F(ab’)2 anti-rabbit IgG alkaline phosphatase and bands were detected using the Tropix WesternStar method. The data show that only the phosphopeptide corresponding to ab4801 blocks the antibody signal, thereby demonstrating the specificity of the antibody.