Mouse FAK (phospho Y397) peptide (ab40145)
- Datasheet
- References
- Protocols
Overview
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Product nameMouse FAK (phospho Y397) peptide
See all FAK proteins and peptides
Description
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NatureSynthetic
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Amino Acid Sequence
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SpeciesMouse
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Specifications
Our Abpromise guarantee covers the use of ab40145 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Blocking
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FormLiquid
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Additional notes
- First try to dissolve a small amount of peptide in either water or buffer. The more charged residues on a peptide, the more soluble it is in aqueous solutions.
- If the peptide doesn’t dissolve try an organic solvent e.g. DMSO, then dilute using water or buffer.
- Consider that any solvent used must be compatible with your assay. If a peptide does not dissolve and you need to recover it, lyophilise to remove the solvent.
- Gentle warming and sonication can effectively aid peptide solubilisation. If the solution is cloudy or has gelled the peptide may be in suspension rather than solubilised.
- Peptides containing cysteine are easily oxidised, so should be prepared in solution just prior to use. -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Information available upon request.
General Info
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Alternative names
- FADK
- FADK 1
- FAK related non kinase polypeptide
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FunctionNon-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. Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly. Plays a potential role in oncogenic transformations resulting in increased kinase activity.
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Tissue specificityExpressed in all organs tested, in lymphoid cell lines, but most abundantly in brain.
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Sequence similaritiesBelongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily.
Contains 1 FERM domain.
Contains 1 protein kinase domain. -
DomainThe first Pro-rich domain interacts with the SH3 domain of CRK-associated substrate (BCAR1) and CASL.
The carboxy-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions. -
Post-translational
modificationsPhosphorylated on 6 tyrosine residues upon activation. Microtubule-induced dephosphorylation at Tyr-397 could be catalyzed by PTPN11 and regulated by ZFYVE21. Dephosphorylated by PTPN11 upon EPHA2 activation by its ligand EFNA1. -
Cellular localizationCell junction > focal adhesion. Cell membrane. Constituent of focal adhesions.
- Information by UniProt
Images
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Blocking - Mouse FAK (phospho Y397) peptide (ab40145)This image is courtesy of an anonymous AbreviewTo demonstrate the specificity of the phosphorylation site specific antibody (ab4803) a 1/150 dilution of anti human-FAK (phospho Y397) antibody was pre-incubated with 200 fold molar excess of peptide (ab40145, 1/15 dilution) for 12 hours rolling at 4°C.
Human Tissue sections (kidney) were deparaffinized, rehydrated and antigen retrieval was performed using citrate buffer pH 6.0. Endogenous peroxidase was quenched using 3% hydrogenperoxide in methanol and blocking was performed. Primary antibody alone (positive control) or mixed with peptide (blocking control) or antibody diluent alone (negative control) was applied to tissue sections and incubated for 16 hours at 4°C. Detection was performed using a HRP detection system. Nuclei were counterstained using Hematoxylin.
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Western blot - FAK (phospho Y397) antibody (ab39967) -
Western blot - Mouse FAK (phospho Y397) peptide (ab40145)
Datasheets and documents
References
ab40145 has not yet been referenced specifically in any publications.
