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AB38512

Anti-FAK (phospho Y925) 抗体

Anti-FAK (phospho Y925) antibody

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(10 Publications)

Rabbit Polyclonal FAK phospho Y925 antibody. Suitable for WB and reacts with Human samples. Cited in 10 publications. Immunogen corresponding to Synthetic Peptide within Human PTK2 pY925 aa 850 to C-terminus.

別名を表示する

FAK, FAK1, PTK2, Focal adhesion kinase 1, FADK 1, Focal adhesion kinase-related nonkinase, Protein phosphatase 1 regulatory subunit 71, Protein-tyrosine kinase 2, p125FAK, pp125FAK, FRNK, PPP1R71

1 Images
Western blot - Anti-FAK (phospho Y925) antibody (AB38512)
  • WB

Unknown

Western blot - Anti-FAK (phospho Y925) antibody (AB38512)

Lanes can be loaded with 5-30µg of total protein.

All lanes:

Western blot - Anti-FAK (phospho Y925) antibody (ab38512) at 1/500 dilution

Lane 1:

HepG2 cell lysate, pre-incubated with phosphopeptide at 30 µg

Lane 2:

HepG2 cell lysate at 30 µg

Lane 3:

293 cell lysate + EGF + serum at 30 µg

Secondary

All lanes:

Alkaline Phosphatase AffiniPure Goat Anti-Rabbit IgG (H+L)

Predicted band size: 119 kDa

Observed band size: 123 kDa

false

Key facts

宿主種

Rabbit

クローン性

Polyclonal

アイソタイプ

IgG

キャリアフリー

No

交差種

Human

アプリケーション

WB

applications

免疫原

Synthetic Peptide within Human PTK2 pY925 aa 850 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

Q05397

Reactivity data

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出荷温度及び保存条件

製品の状態
Liquid
精製方法
Affinity purification Immunogen
精製に関する特記事項
The antibody was affinity purified from rabbit antiserum by affinity chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
バッファー組成
pH: 7.4 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride
出荷温度
Blue Ice
短期保存温度
+4°C
長期保存温度
-20°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

Focal Adhesion Kinase (FAK) also known as Protein Tyrosine Kinase 2 (PTK2) is a non-receptor tyrosine kinase. This protein has a molecular weight of approximately 125 kDa. FAK is expressed at high levels in brain muscle and liver tissues. Mechanically FAK plays a role in cellular adhesion and migration by regulating integrin signaling and cell-extracellular matrix interactions. FAK auto-phosphorylates at tyrosine residue 397 creating a binding site for Src family kinases and promoting downstream signaling pathways.
Biological function summary

Focal Adhesion Kinase participates in the formation of focal adhesions which are complexes that connect the cytoskeleton to the extracellular matrix. The FAK protein functions as an important signaling node in these structures allowing for the assembly of multiprotein signal transduction complexes. FAK also controls cellular processes such as spreading motility and survival. The interaction with proteins such as Src kinases paxillin and talin facilitates its biological roles in cell signaling.

Pathways

Focal Adhesion Kinase engages in the regulation of the MAPK/ERK signaling pathway and the PI3K/AKT pathway. These pathways are instrumental for cell proliferation survival and migration. In these pathways FAK interacts with proteins such as PI3K Grb2 and Sos linking integrin-mediated signals with downstream effects that influence cell behavior and survival.

Altered FAK signaling has ties to cancer progression and metastasis as well as cardiovascular diseases. In cancer the overexpression of FAK and its interaction with proteins like Src and VEGFR can drive tumor growth and angiogenesis. In cardiovascular diseases improper FAK activation can lead to aberrant heart tissue remodeling and associated pathologies. Abnormalities in FAK signaling pathways can therefore contribute significantly to the development and progression of these diseases.

製品プロトコール

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ターゲットの情報

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. Phosphorylates NEDD9 following integrin stimulation (PubMed : 9360983). 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.
See full target information PTK2 pY925

文献 (10)

Recent publications for all applications. Explore the full list and refine your search

The Journal of cell biology 223: PubMed38466167

2024

Paxillin phase separation promotes focal adhesion assembly and integrin signaling.

Applications

Unspecified application

Species

Unspecified reactive species

Peigang Liang,Yuchen Wu,Shanyuan Zheng,Jiaqi Zhang,Shuo Yang,Jinfang Wang,Suibin Ma,Mengjun Zhang,Zhuang Gu,Qingfeng Liu,Wenxue Jiang,Qiong Xing,Bo Wang

EMBO reports 24:e56850 PubMed37846507

2023

An ULK1/2-PXN mechanotransduction pathway suppresses breast cancer cell migration.

Applications

Unspecified application

Species

Unspecified reactive species

Peigang Liang,Jiaqi Zhang,Yuchen Wu,Shanyuan Zheng,Zhaopeng Xu,Shuo Yang,Jinfang Wang,Suibin Ma,Li Xiao,Tianhui Hu,Wenxue Jiang,Chaoqun Huang,Qiong Xing,Mondira Kundu,Bo Wang

Cell reports 34:108876 PubMed33761359

2021

Paradoxical activation of c-Src as a drug-resistant mechanism.

Applications

Unspecified application

Species

Unspecified reactive species

Makio Higuchi,Kenichi Ishiyama,Masahiro Maruoka,Ryosuke Kanamori,Akifumi Takaori-Kondo,Naoki Watanabe

OncoTargets and therapy 12:10415-10425 PubMed31819523

2019

Recombinant Viral Capsid Protein L2 (rVL2) of HPV 16 Suppresses Cell Proliferation and Glucose Metabolism via ITGB7/C/EBPβ Signaling Pathway in Cervical Cancer Cell Lines.

Applications

Unspecified application

Species

Unspecified reactive species

Zhihong Chai,Yufei Yang,ZhongYi Gu,Xianli Cai,Wenwei Ye,Lin Kong,Xiaoxiao Qiu,Lingxiao Ying,Ziliang Wang,Linyou Wang

Oncotarget 8:21674-21691 PubMed28423510

2017

Genistein inhibits the growth and regulates the migration and invasion abilities of melanoma cells via the FAK/paxillin and MAPK pathways.

Applications

Unspecified application

Species

Unspecified reactive species

Shuna Cui,Juan Wang,Qingqing Wu,Jing Qian,Changshui Yang,Ping Bo

The EMBO journal 34:448-65 PubMed25471072

2014

KSHV-TK is a tyrosine kinase that disrupts focal adhesions and induces Rho-mediated cell contraction.

Applications

Unspecified application

Species

Unspecified reactive species

Michael B Gill,Rachel Turner,Philip G Stevenson,Michael Way

Biochimica et biophysica acta 1853:388-95 PubMed25450971

2014

Imatinib restores VASP activity and its interaction with Zyxin in BCR-ABL leukemic cells.

Applications

Unspecified application

Species

Unspecified reactive species

Vanessa A Bernusso,João A Machado-Neto,Fernando V Pericole,Karla P Vieira,Adriana S S Duarte,Fabiola Traina,Marc D Hansen,Sara T Olalla Saad,Karin S A Barcellos

PloS one 9:e92597 PubMed24675668

2014

Novel anti-microbial peptide SR-0379 accelerates wound healing via the PI3 kinase/Akt/mTOR pathway.

Applications

WB

Species

Rat

Hideki Tomioka,Hironori Nakagami,Akiko Tenma,Yoshimi Saito,Toshihiro Kaga,Toshihide Kanamori,Nao Tamura,Kazunori Tomono,Yasufumi Kaneda,Ryuichi Morishita

Stem cells translational medicine 3:481-8 PubMed24558164

2014

Mesenchymal stem cells with modification of junctional adhesion molecule a induce hair formation.

Applications

Unspecified application

Species

Unspecified reactive species

Minjuan Wu,Xiaocan Guo,Ling Yang,Yue Wang,Ying Tang,Yongji Yang,Houqi Liu

PLoS pathogens 7:e1002346 PubMed22102809

2011

Murid herpesvirus-4 exploits dendritic cells to infect B cells.

Applications

ICC/IF

Species

Mouse

Miguel Gaspar,Janet S May,Soumi Sukla,Bruno Frederico,Michael B Gill,Christopher M Smith,Gabrielle T Belz,Philip G Stevenson
View all publications

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