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Merck
CN

05-1140

Anti-phospho-Focal Adhesion Kinase (Tyr397) Antibody, clone 18

clone 18, from mouse

别名:

FADK 1, PTK2 protein tyrosine kinase 2, Protein-tyrosine kinase 2, focal adhesion kinase 1

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Clone:
18, monoclonal
Species reactivity:
mouse, human
Application:
western blot
Technique(s):
western blot: suitable
Citations:
12
Uniprot accession no.:
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产品名称

Anti-phospho-Focal Adhesion Kinase (Tyr397) Antibody, clone 18, clone 18, from mouse

biological source

mouse

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

18, monoclonal

species reactivity

mouse, human

technique(s)

western blot: suitable

isotype

IgG1

UniProt accession no.

shipped in

wet ice

target post-translational modification

phosphorylation (pTyr397)

Quality Level

Gene Information

human ... PTK2(5747)
mouse ... Ptk2(14083)

Analysis Note

Control
LPS treated RAW 264 lysates.
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.

Application

Research Category
Cell Structure
Research Sub Category
Cytoskeletal Signaling
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).

Biochem/physiol Actions

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.

Disclaimer

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.

General description

125 kDa
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.

Immunogen

Epitope: Tyrosine 397
Generated from human FAK, a.a. 393-404, phosphorylated on Tyr397.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Replaces: 04-974

Physical form

Format: Purified
Protein A purified
Purified mouse monoclonal IgG1 in aqueous buffered solution containing 50% glycerol, BSA, and <0.09% sodium azide.

Preparation Note

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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存储类别

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Melisa J Andrade et al.
Journal of cell science, 134(12) (2021-06-18)
UVBR-induced photolesions in genomic DNA of keratinocytes impair cellular functions and potentially determine the cell fate post-irradiation. The ability of insulin-like growth factor-I (IGF-I) to rescue epidermal keratinocytes after photodamage via apoptosis prevention and photolesion removal was recently demonstrated using
Rafaela Muniz de Queiroz et al.
Nature communications, 15(1), 7132-7132 (2024-08-21)
Although the E3 ligase Mdm2 and its homologue and binding partner MdmX are the major regulators of the p53 tumor suppressor protein, it is now evident that Mdm2 and MdmX have multiple functions that do not involve p53. As one
Catherine Moorwood et al.
Skeletal muscle, 4, 13-13 (2014-07-16)
The dystrophin glycoprotein complex (DGC) is located at the sarcolemma of muscle fibers, providing structural integrity. Mutations in and loss of DGC proteins cause a spectrum of muscular dystrophies. When only the sarcoglycan subcomplex is absent, muscles display severe myofiber
Jorge Carretero-Ortega et al.
eLife, 8 (2019-05-06)
Semaphorins (SEMAs) and their Plexin (PLXN) receptors are central regulators of metazoan cellular communication. SEMA-PLXND1 signaling plays important roles in cardiovascular, nervous, and immune system development, and cancer biology. However, little is known about the molecular mechanisms that modulate SEMA-PLXND1
Konstantina Karamanou et al.
The FEBS journal, 287(22), 4862-4880 (2020-03-12)
The small leucine-rich proteoglycan lumican regulates estrogen receptors (ERs)-associated functional properties of breast cancer cells, expression of matrix macromolecules, and epithelial-to-mesenchymal transition. However, it is not known whether the ER-dependent lumican effects on breast cancer cells are related to the

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