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05-1140

Sigma-Aldrich

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

clone 18, from mouse

Synonyme(s) :

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

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

18, monoclonal

Espèces réactives

mouse, human

Technique(s)

western blot: suitable

Isotype

IgG1

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

phosphorylation (pTyr397)

Informations sur le gène

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

Description générale

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.

Spécificité

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.

Immunogène

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

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).

Qualité

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.

Description de la cible

125 kDa

Liaison

Replaces: 04-974

Forme physique

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

Stockage et stabilité

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.

Remarque sur l'analyse

Control
LPS treated RAW 264 lysates.

Autres remarques

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

Clause de non-responsabilité

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.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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
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
Derek L Clouthier et al.
Molecular and cellular biology, 35(9), 1573-1587 (2015-02-19)
Development of the cardiovascular system is critically dependent on the ability of endothelial cells (ECs) to reorganize their intracellular actin architecture to facilitate migration, adhesion, and morphogenesis. Nck family cytoskeletal adaptors function as key mediators of actin dynamics in numerous
Christoph Seiler et al.
PLoS biology, 10(9), e1001386-e1001386 (2012-09-14)
The signals that initiate cell invasion are not well understood, but there is increasing evidence that extracellular physical signals play an important role. Here we show that epithelial cell invasion in the intestine of zebrafish meltdown (mlt) mutants arises in
Ling Guo et al.
Nature communications, 10(1), 845-845 (2019-02-21)
Cell metabolism is strongly influenced by mechano-environment. We show here that a fraction of kindlin-2 localizes to mitochondria and interacts with pyrroline-5-carboxylate reductase 1 (PYCR1), a key enzyme for proline synthesis. Extracellular matrix (ECM) stiffening promotes kindlin-2 translocation into mitochondria

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