FAK plays a central role in cell spreading, differentiation, migration, cell death and acceleration of the G1 to S phase transition of the cell cycle. FAK regulation includes phosphorylation at multiple tyrosine and serine residues. Phosphorylation of tyrosine generally is associated with positive regulation and growth promotion, however, dephosphorylation at these sites occurs as cells enter mitosis (M-Phase of the cell cycle). In contrast, serine phosphorylation either remains high or is increased as cells enter mitosis and may play a role in focal adhesion disassembly. Tyrosine 397 is the autophosphorylation site of Focal Adhesion Kinase. The site binds Src family SH2 domains and the p85 subunit of PI3-Kinase.
Product Information
Format
Purified
Control
LPS treated RAW 264 lysates.
Presentation
Purified mouse monoclonal IgG1 in aqueous buffered solution containing 50% glycerol, BSA, and < 0.09% sodium azide.
Applications
Application
This Anti-phospho-Focal Adhesion Kinase (Tyr397) Antibody, clone 18 is validated for use in WB for the detection of phospho-Focal Adhesion Kinase (Tyr397).
Key Applications
Western Blotting
Biological Information
Immunogen
Generated from human FAK, a.a. 393-404, phosphorylated on Tyr397.
Epitope
Tyrosine 397
Clone
18
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Mouse
Specificity
Reacts specifically with Focal Adhesion Kinase (FAK) when phosphorylated on Tyr397. FAK is a cytoplasmic tyrosine kinase that colocalizes with integrins in focal adhesions. This cellular localization is directed by a 125 amino acid sequence at the C-terminus called the "Focal Adhesion Targeting" sequence (FAT). The binding of extracellular matrix ligands to integrins triggers autophosphorylation at Tyr-397, and activation of FAK through phosphorylation of Tyr residues (Tyr-576 and Tyr577) in the kinase domain activation loop.
FUNCTION:Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Plays a potential role in oncogenic transformations resulting in increased kinase activity. CATALYTIC ACTIVITY:ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. SUBUNIT STRUCTURE:Interacts with CAS family members and with GIT1, SORBS1 and BCAR3. Interacts with RGNEF and SHB By similarity. Interacts with TGFB1I1 and STEAP4. SUBCELLULAR LOCATION:Cell junction › focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Constituent of focal adhesions. TISSUE SPECIFICITY:Expressed in all organs tested, in lymphoid cell lines, but most abundantly in brain. DOMAIN:The first Pro-rich domain interacts with the SH3 domain of CRK-associated substrate (BCAR1) and CASL By similarity.
The carboxy-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions. PTM:Phosphorylated on 6 tyrosine residues upon activation. SEQUENCE SIMILARITIES:Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily.
Contains 1 FERM domain.
Contains 1 protein kinase domain.
Product Usage Statements
Quality Assurance
Evaluated by Western Blot in LPS treated RAW 264 lysates.
Western Blot Analysis: 1:500 dilution of this lot detected phospho-FAK (Tyr397) on 10 ug of LPS treated RAW 264 lysates.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20ºC from date of receipt.
Note: Variability in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.
FAK plays a central role in cell spreading, differentiation, migration, cell death and acceleration of the G1 to S phase transition of the cell cycle. FAK regulation includes phosphorylation at multiple tyrosine and serine residues. Phosphorylation of tyrosine generally is associated with positive regulation and growth promotion, however, dephosphorylation at these sites occurs as cells enter mitosis (M-Phase of the cell cycle). In contrast, serine phosphorylation either remains high or is increased as cells enter mitosis and may play a role in focal adhesion disassembly. Tyrosine 397 is the autophosphorylation site of Focal Adhesion Kinase. The site binds Src family SH2 domains and the p85 subunit of PI3-Kinase.
Product Information
Format
Purified
Control
LPS treated RAW 264 lysates.
Presentation
Purified mouse monoclonal IgG1 in aqueous buffered solution containing 50% glycerol, BSA, and < 0.09% sodium azide.
Applications
Application
This Anti-phospho-Focal Adhesion Kinase (Tyr397) Antibody, clone 18 is validated for use in WB for the detection of phospho-Focal Adhesion Kinase (Tyr397).
Key Applications
Western Blotting
Biological Information
Immunogen
Generated from human FAK, a.a. 393-404, phosphorylated on Tyr397.
Epitope
Tyrosine 397
Clone
18
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Mouse
Specificity
Reacts specifically with Focal Adhesion Kinase (FAK) when phosphorylated on Tyr397. FAK is a cytoplasmic tyrosine kinase that colocalizes with integrins in focal adhesions. This cellular localization is directed by a 125 amino acid sequence at the C-terminus called the "Focal Adhesion Targeting" sequence (FAT). The binding of extracellular matrix ligands to integrins triggers autophosphorylation at Tyr-397, and activation of FAK through phosphorylation of Tyr residues (Tyr-576 and Tyr577) in the kinase domain activation loop.
FUNCTION:Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Plays a potential role in oncogenic transformations resulting in increased kinase activity. CATALYTIC ACTIVITY:ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. SUBUNIT STRUCTURE:Interacts with CAS family members and with GIT1, SORBS1 and BCAR3. Interacts with RGNEF and SHB By similarity. Interacts with TGFB1I1 and STEAP4. SUBCELLULAR LOCATION:Cell junction › focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Constituent of focal adhesions. TISSUE SPECIFICITY:Expressed in all organs tested, in lymphoid cell lines, but most abundantly in brain. DOMAIN:The first Pro-rich domain interacts with the SH3 domain of CRK-associated substrate (BCAR1) and CASL By similarity.
The carboxy-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions. PTM:Phosphorylated on 6 tyrosine residues upon activation. SEQUENCE SIMILARITIES:Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily.
Contains 1 FERM domain.
Contains 1 protein kinase domain.
Product Usage Statements
Quality Assurance
Evaluated by Western Blot in LPS treated RAW 264 lysates.
Western Blot Analysis: 1:500 dilution of this lot detected phospho-FAK (Tyr397) on 10 ug of LPS treated RAW 264 lysates.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20ºC from date of receipt.
Note: Variability in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.
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