Lane 1: Hela cell lysate
Lane 2: mouse spleen tissue lysate
Lane 3: 293T cell lysate
Lane 4: A431 cell lysate
Recombinant Rabbit monoclonal primary
Recombinant FAK Monoclonal Antibody (ET1602-25)
Synthetic peptide within human fak aa 700-740.
Hela cell lysate, mouse spleen tissue lysate, 293T cell lysate, A431 cell lysate, PANC-1, SH-SY5Y, human liver carcinoma tissue, human spleen tissue, human kidney tissue, mouse brain tissue, mouse spleen tissue, mouse kidney tissue, Hela.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
FADK 1 antibody; FADK antibody; FAK related non kinase polypeptide antibody; FAK1 antibody; FAK1_HUMAN antibody; Focal adhesion kinase 1 antibody; Focal adhesion Kinase antibody; Focal adhesion kinase isoform FAK Del33 antibody; Focal adhesion kinase related nonkinase antibody; FRNK antibody; p125FAK antibody; pp125FAK antibody; PPP1R71 antibody; Protein phosphatase 1 regulatory subunit 71 antibody; Protein tyrosine kinase 2 antibody; Protein-tyrosine kinase 2 antibody; Ptk2 antibody; PTK2 protein tyrosine kinase 2 antibody
Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily.
Detected in B and T-lymphocytes. Isoform 1 and isoform 6 are detected in lung fibroblasts (at protein level). Ubiquitous. Expressed in epithelial cells (at protein level).
[Isoform 6]: Detected in cultured cells, immediately after seeding and before formation of focal adhesions (at protein level).
Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity).; Sumoylated; this enhances autophosphorylation.
Cytoplasm, Nucleus, Cell membrane, Cell junction.
Focal adhesion kinase was initially identified as a major substrate for the intrinsic protein tyrosine kinase activity of Src encoded pp60. The deduced amino acid sequence of FAK p125 has shown it to be a cytoplasmic protein tyrosine kinase whose sequence and structural organization are unique as compared to other proteins described to date. Localization of p125 by immunofluorescence suggests that it is primarily found in cellular focal adhesions leading to its designation as focal adhesion kinase (FAK). FAK is concentrated at the basal edge of only those basal keratinocytes that are actively migrating and rapidly proliferating in repairing burn wounds and is activated and localized to the focal adhesions of spreading keratinocytes in culture. Thus, it has been postulated that FAK may have an important in vivo role in the reepithelialization of human wounds. FAK protein tyrosine kinase activity has also been shown to increase in cells stimulated to grow by use of mitogenic neuropeptides or neurotransmitters acting through G protein coupled receptors.
Xu, Xiu-Ping et al.
Ang II-AT2R increases mesenchymal stem cell migration by signaling through the FAK and RhoA/Cdc42 pathways in vitro. | Stem Cell Research & Therapy