Human FGFR2 alpha Antibody Summary
Arg22-Glu377
Accession # P21802.1
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Detection of FGFR2 alpha in HT‑29 (Positive) and HEL 92.1.7 (Negative). FGFR2 alpha was detected in immersion fixed HT‑29 Human Colon Adenocarcinoma Cell Line (Positive) and absent in HEL 92.1.7 Human Erythroleukemic Cell Line (Negative) using Mouse Anti-Human FGFR2 alpha Monoclonal Antibody (Catalog # MAB11119) at 3 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
Detection of FGFR2 alpha in KatoIII cells by Flow Cytometry. KATO‑III human gastric carcinoma cells were stained with Mouse Anti-Human FGFR2 alpha Monoclonal Antibody (Catalog # MAB11119, filled histogram) or isotype control antibody (Catalog # MAB004, open histogram), followed by Allophycocyanin-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # F0101B). View our protocol for Staining Membrane-associated Proteins.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: FGFR2 alpha
Fibroblast growth factor receptor 2 (FGFR2) belongs to a family of type I transmembrane tyrosine kinases which mediate the biological functions of FGFs that are involved in a multitude of physiological and pathological cellular processes (1). The FGFR family is comprised of 4 structurally conserved members (FGFR1-4) all possessing an extracellular domain (ECD) with three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and cytoplasmic split tyrosine-kinase domain (1, 2). The ECD of mature, full-length FGFR2 shares 95% amino acid sequence identity with mouse FGFR2. Alternative splicing generates multiple forms of FGFR1-3, each with unique signaling characteristics (1-3). For FGFR2, alternative splicing of the ECD, specifically the IgIII domain, results in IIIb, or IIIc isoforms (4). The FGFR splice variants also exhibit distinct and varying binding affinities for different FGF ligands (2, 4). Specifically, FGFR2A (IIIc) binds most FGF ligands but not the FGF10 subfamily, while FGFR2A (IIIc) binds only members of the FGF10 subfamily (5). FGFRs mediate the FGF signaling cascade which regulate developmental processes including cellular proliferation, differentiation, and migration, morphogenesis, and patterning (6). FGFRs transduce the signals through three dominant pathways including RAS/MAPK, PI3k/AKT, and PLC gamma (7). While FGFR2 is widely expressed in many adult human tissues, isoform expression is tissue specific, with IIIb predominantly expressed in epithelial cells, while IIIc is expressed in mesenchymal cells (5). FGFR2 signaling is critical for embryonic development, tissue repair, and regulation of osteoblast function and bone growth (8). Mutations in FGFR2 or misregulation of FGFR2 mediated signaling is found in multiple skeletal dysplasias, with FGFR2A (IIIc) specifically upregulated in several cancers including prostate, breast and pancreatic and is proposed as a novel therapeutic target for colorectal carcinomas (6, 9).
- Ornitz, D.M. and Itoh, N. (2015) Wiley Interdiscip Rev Dev Biol. 4:215.
- Zhang, X. et al. (2006) J Biol Chem. 281:15694.
- Ferguson, H.R. et al. (2021) Signaling. Cells 10:1201.
- Holzmann, K. et al. (2012) J Nucleic Acids. 2012:950508.
- Wagner, E.J. et al. (2003) RNA 9:1552.
- Xie, Y. et al. (2020) Sig Transduct Target Ther 5:181.
- Mossahebi-Mohammadi, M. et al. (2020) Front Cell Dev Biol. 18:79.
- Teven, C.M. et al. (2014) Genes Dis. 1:199.
- Matsuda, Y. et al. (2012) Mol Cancer Ther. 11:2010.
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