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Mouse Anti-FER Recombinant Antibody (CBXF-0499) (CBMAB-F2304-CQ)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBXF-0499
Antibody Isotype
IgG1
Application
IP, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4, 1% BSA
Preservative
0.05% sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
FER Tyrosine Kinase
Introduction
The protein encoded by this gene is a member of the FPS/FES family of non-transmembrane receptor tyrosine kinases. It regulates cell-cell adhesion and mediates signaling from the cell surface to the cytoskeleton via growth factor receptors. Alternative splicing results in multiple transcript variants. A related pseudogene has been identified on chromosome X.
Entrez Gene ID
2241
UniProt ID
P16591
Alternative Names
FER Tyrosine Kinase; Fujinami Poultry Sarcoma/Feline Sarcoma-Related Protein Fer; Protein Phosphatase 1, Regulatory Subunit 74; Feline Encephalitis Virus-Related Kinase FER; Fer (Fps/Fes Related) Tyrosine Kinase; Phosphoprotein NCP94; Proto-Oncogene C-Fer; Tyrosine Kinase 3;
Research Area
Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Plays a role in synapse organization, trafficking of synaptic vesicles, the generation of excitatory postsynaptic currents and neuron-neuron synaptic transmission. Plays a role in neuronal cell death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3, but the biological relevance of this depends on cell type and stimulus.
Biological Process
Actin cytoskeleton reorganization Source: UniProtKB
Cell adhesion Source: GO_Central
Cell-cell adhesion mediated by cadherin Source: UniProtKB
Cell differentiation Source: GO_Central
Cell population proliferation Source: InterPro
Cellular response to insulin stimulus Source: UniProtKB
Cellular response to macrophage colony-stimulating factor stimulus Source: UniProtKB
Cellular response to reactive oxygen species Source: UniProtKB
Chemotaxis Source: GO_Central
Cytokine-mediated signaling pathway Source: UniProtKB
Diapedesis Source: UniProtKB
Extracellular matrix-cell signaling Source: UniProtKB
Fc-epsilon receptor signaling pathway Source: UniProtKB
Innate immune response Source: GO_Central
Insulin receptor signaling pathway via phosphatidylinositol 3-kinase Source: UniProtKB
Interleukin-6-mediated signaling pathway Source: UniProtKB
Intracellular signal transduction Source: ProtInc
Kit signaling pathway Source: UniProtKB
Microtubule cytoskeleton organization Source: UniProtKB
Negative regulation of mast cell activation involved in immune response Source: UniProtKB
Peptidyl-tyrosine phosphorylation Source: UniProtKB
Platelet-derived growth factor receptor signaling pathway Source: UniProtKB
Positive regulation of actin filament polymerization Source: UniProtKB
Positive regulation of cell migration Source: UniProtKB
Positive regulation of cell population proliferation Source: CACAO
Positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
Protein autophosphorylation Source: UniProtKB
Protein phosphorylation Source: ProtInc
Regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
Regulation of fibroblast migration Source: Ensembl
Regulation of lamellipodium assembly Source: UniProtKB
Regulation of mast cell degranulation Source: GO_Central
Regulation of protein phosphorylation Source: UniProtKB
Response to lipopolysaccharide Source: UniProtKB
Response to platelet-derived growth factor Source: UniProtKB
Substrate adhesion-dependent cell spreading Source: UniProtKB
Transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
Tyrosine phosphorylation of STAT protein Source: UniProtKB
Cellular Location
Cell membrane; Nucleus; Cytoplasm; Cytoskeleton; Cell projection; Cell junction; Membrane; Cell cortex. Associated with the chromatin. Detected on microtubules in polarized and motile vascular endothelial cells. Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1 and CTNND1 at nascent cell-cell contacts.
PTM
Autophosphorylated.
Polyubiquitinated; this leads to proteasomal degradation.
More Infomation

Grinshtain, E., Shpungin, S., Baum, M., Nir, U., & Breitbart, H. (2022). The Fer tyrosine kinase protects sperm from spontaneous acrosome reaction. Developmental Biology, 487, 24-33.

Zhang, Y., Xiong, X., Zhu, Q., Zhang, J., Chen, S., Wang, Y., ... & Fan, G. (2022). FER-mediated phosphorylation and PIK3R2 recruitment on IRS4 promotes AKT activation and tumorigenesis in ovarian cancer cells. Elife, 11, e76183.

Lonic, A., Gehling, F., Belle, L., Li, X., Schieber, N. L., Nguyen, E. V., ... & Khew-Goodall, Y. (2021). Phosphorylation of PKCδ by FER tips the balance from EGFR degradation to recycling. Journal of Cell Biology, 220(2).

Debackere, K., van der Krogt, J. A., Tousseyn, T., Ferreiro, J. A. F., Van Roosbroeck, K., Marcelis, L., ... & Wlodarska, I. (2020). FER and FES tyrosine kinase fusions in follicular T-cell lymphoma. Blood, The Journal of the American Society of Hematology, 135(8), 584-588.

Ivanova, I. A., Arulanantham, S., Barr, K., Cepeda, M., Parkins, K. M., Hamilton, A. M., ... & Dagnino, L. (2019). Targeting FER kinase inhibits melanoma growth and metastasis. Cancers, 11(3), 419.

Taniguchi, T., Inagaki, H., Baba, D., Yasumatsu, I., Toyota, A., Kaneta, Y., ... & Nakayama, K. (2019). Discovery of novel pyrido-pyridazinone derivatives as FER tyrosine kinase inhibitors with antitumor activity. ACS medicinal chemistry letters, 10(5), 737-742.

Matsuura, Y. (2019). High‐resolution structural analysis shows how different crystallographic environments can induce alternative modes of binding of a phosphotyrosine peptide to the SH2 domain of Fer tyrosine kinase. Protein Science, 28(11), 2011-2019.

Zhang, J., Wang, Z., Zhang, S., Chen, Y., Xiong, X., Li, X., ... & Fan, G. (2018). Spatial regulation of signaling by the coordinated action of the protein tyrosine kinases MET and FER. Cellular signalling, 50, 100-110.

Yamamoto, H., Kondo, A., & Itoh, T. (2018). A curvature-dependent membrane binding by tyrosine kinase Fer involves an intrinsically disordered region. Biochemical and biophysical research communications, 495(1), 1522-1527.

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For research use only. Not intended for any clinical use.

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