Recombinant human PYK2 protein is a Human Full Length protein, expressed in Baculovirus infected Sf9, with >=62% purity and suitable for SDS-PAGE, Inhib.
| Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application Inhib | Reactivity Reacts | Dilution info - | Notes - |
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Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376'. Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2.
FAK2, PYK2, RAFTK, PTK2B, Protein-tyrosine kinase 2-beta, Calcium-dependent tyrosine kinase, Calcium-regulated non-receptor proline-rich tyrosine kinase, Cell adhesion kinase beta, Focal adhesion kinase 2, Proline-rich tyrosine kinase 2, Related adhesion focal tyrosine kinase, CADTK, CAK-beta, CAKB, FADK 2
Recombinant human PYK2 protein is a Human Full Length protein, expressed in Baculovirus infected Sf9, with >=62% purity and suitable for SDS-PAGE, Inhib.
pH: 8
Constituents: 50% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.395% Tris HCl, 0.05% Sorbitan monolaurate, ethoxylated, 0.0462% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
Affinity purified.
Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376'. Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2.
Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily.
Phosphorylated on tyrosine residues in response to various stimuli that elevate the intracellular calcium concentration; this activation is indirect and may be mediated by production of reactive oxygen species (ROS). Tyr-402 is the major autophosphorylation site, but other kinases can also phosphorylate Tyr-402. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-402 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-579; Tyr-580 and Tyr-881. Phosphorylation at Tyr-881 is important for interaction with GRB2. Phosphorylated on tyrosine residues upon activation of FGR and PKC. Recruitment by NPHP1 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. Phosphorylation by MYLK promotes ITGB2 activation and is thus essential to trigger neutrophil transmigration during lung injury. Dephosphorylated by PTPN12.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Source : Baculovirus infected Sf9 cells
PYK2 also known as Protein Tyrosine Kinase 2 Beta (PTK2B) is a protein with a mass of approximately 116 kDa. This enzyme belongs to the focal adhesion kinase (FAK) family and functions as a non-receptor protein tyrosine kinase. Mechanically PYK2 is involved in calcium-dependent signaling and is activated by increases in intracellular calcium levels. It plays a critical role in cell proliferation migration and survival. PYK2 expresses widely in neuronal tissues hematopoietic cells and various epithelial cells.
PYK2 interacts with integrins and G-protein-coupled receptors (GPCRs) linking extracellular signals to intracellular pathways. It forms complexes with other signaling molecules including Rac1 and c-Src facilitating downstream signaling. These interactions contribute to cellular communication and adhesion processes especially in the central nervous system and immune cells. Through its involvement in signal transduction PYK2 supports cellular responses to environmental changes.
PYK2 participates in the MAPK and JNK signaling pathways. These pathways are critical for transmitting signals from the cell surface to the nucleus influencing cellular growth and stress responses. PYK2 interacts closely with other proteins such as Src and FAK which help coordinate signals that regulate cellular dynamics. Through these pathways PYK2 modulates processes involved in the structural reorganization of cells and tissues.
PYK2 has been linked to neurodegenerative diseases and certain types of cancers. In Alzheimer's disease PYK2 may contribute to synaptic dysfunction and cognitive decline as it interacts with amyloid-beta peptides and tau proteins. In cancer PYK2 overexpression can promote cancer cell invasion metastasis and resistance to apoptosis often in coordination with proteins like FAK. Therefore understanding the role of PYK2 in these conditions provides insights for therapeutic developments.
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