Mouse Anti-PTK2 (Phosphorylated Y397) Recombinant Antibody (6D382) (PTM-CBMAB-0445LY)

Mouse

Human, Mouse

6D382

IgG1

ELISA, WB

Synthetic phosphopeptide corresponding to a portion of FAK (focal adhesion kinase) phosphorylated at Tyr397

Human, Mouse

IgG1

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Liquid

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

protein tyrosine kinase 2

Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. 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 the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription.
Isoform 6
Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription.

AngiogenesisManual Assertion Based On ExperimentIBA:GO_Central
Axon guidanceManual Assertion Based On ExperimentTAS:UniProtKB
Cell differentiationManual Assertion Based On ExperimentIBA:GO_Central
Cell migrationManual Assertion Based On ExperimentIMP:BHF-UCL
Cell motilityManual Assertion Based On ExperimentTAS:UniProtKB
Detection of muscle stretchManual Assertion Based On ExperimentTAS:BHF-UCL
Ephrin receptor signaling pathwayManual Assertion Based On ExperimentIDA:UniProtKB
Epidermal growth factor receptor signaling pathwayManual Assertion Based On ExperimentIBA:GO_Central
Establishment of cell polarityManual Assertion Based On ExperimentTAS:UniProtKB
Fc-gamma receptor signaling pathway involved in phagocytosisTAS:Reactome
Growth hormone receptor signaling pathwayManual Assertion Based On ExperimentIDA:BHF-UCL
Heart morphogenesisManual Assertion Based On ExperimentTAS:UniProtKB
Innate immune responseManual Assertion Based On ExperimentIBA:GO_Central
Integrin-mediated signaling pathwayManual Assertion Based On ExperimentIDA:UniProtKB
Negative regulation of anoikisManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of apoptotic processManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of cell-cell adhesionManual Assertion Based On ExperimentIDA:BHF-UCL
Netrin-activated signaling pathwayManual Assertion Based On ExperimentTAS:UniProtKB
Peptidyl-tyrosine phosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Placenta developmentManual Assertion Based On ExperimentTAS:UniProtKB
Positive regulation of cell migrationManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of cell population proliferationISS:UniProtKB
Positive regulation of fibroblast migrationManual Assertion Based On ExperimentIDA:ARUK-UCL
Positive regulation of macrophage chemotaxisManual Assertion Based On ExperimentIGI:ARUK-UCL
Positive regulation of macrophage proliferationManual Assertion Based On ExperimentIGI:ARUK-UCL
Positive regulation of phosphatidylinositol 3-kinase activityManual Assertion Based On ExperimentTAS:UniProtKB
Positive regulation of phosphatidylinositol 3-kinase signalingManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of protein kinase activityManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of protein kinase B signalingManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of protein phosphorylationManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of ubiquitin-dependent protein catabolic processISS:UniProtKB
Positive regulation of wound healingManual Assertion Based On ExperimentIDA:ARUK-UCL
Protein autophosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Protein phosphorylationManual Assertion Based On ExperimentIBA:GO_Central
Regulation of cell adhesionManual Assertion Based On ExperimentIBA:GO_Central
Regulation of cell adhesion mediated by integrinManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of cell population proliferationManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of cell shapeManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of cytoskeleton organizationManual Assertion Based On ExperimentTAS:UniProtKB
Regulation of endothelial cell migrationManual Assertion Based On ExperimentTAS:UniProtKB
Regulation of epithelial cell migrationManual Assertion Based On ExperimentIGI:UniProtKB
Regulation of focal adhesion assemblyManual Assertion Based On ExperimentIGI:UniProtKB
Regulation of GTPase activityManual Assertion Based On ExperimentTAS:UniProtKB
Regulation of osteoblast differentiationManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of protein phosphorylationManual Assertion Based On ExperimentIGI:UniProtKB
Regulation of substrate adhesion-dependent cell spreadingManual Assertion Based On ExperimentIGI:UniProtKB
Signal complex assemblyIEA:InterPro
Transforming growth factor beta receptor signaling pathwayManual Assertion Based On ExperimentIDA:UniProtKB
Transmembrane receptor protein tyrosine kinase signaling pathwayManual Assertion Based On ExperimentIBA:GO_Central
Vascular endothelial growth factor receptor signaling pathwayTAS:Reactome

Cell junction, focal adhesion
Cell membrane
Cytoplasm, cell cortex
Cytoplasm, cytoskeleton
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
Nucleus
Cytoplasm, cytoskeleton, cilium basal body
Constituent of focal adhesions. Detected at microtubules.

Aberrant PTK2/FAK1 expression may play a role in cancer cell proliferation, migration and invasion, in tumor formation and metastasis. PTK2/FAK1 overexpression is seen in many types of cancer.

Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity).
Sumoylated; this enhances autophosphorylation.