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Monoclonal Antibody Immunofluorescence Immunocytochemistry Middle Ear Morphogenesis

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Sine oculis homeobox (SIX) proteins belong to a family of evolutionarily conserved transcription factors discovered in Drosophila mutant screens for embryonic eye development genes (1-3). The prototypical family member (sine oculis, so) was named for eyeless embryos carrying mutations in a gene highly conserved among vertebrates, including humans (SIX1) (4). A total of six family members (SIX1-6) have been identified in vertebrates. Each SIX protein contains a homeobox nucleic acid recognition domain (HD) with a DNA-binding helix-turn-helix motif and an adjacent SIX domain, which may be involved in regulating protein-protein interactions (5). In addition to their critical functions during embryonic organogenesis, research studies suggest that SIX proteins play additional roles in postnatal cell cycle regulation, with potentially important implications in tumorigenesis (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Sine oculis homeobox (SIX) proteins belong to a family of evolutionarily conserved transcription factors discovered in Drosophila mutant screens for embryonic eye development genes (1-3). The prototypical family member (sine oculis, so) was named for eyeless embryos carrying mutations in a gene highly conserved among vertebrates, including humans (SIX1) (4). A total of six family members (SIX1-6) have been identified in vertebrates. Each SIX protein contains a homeobox nucleic acid recognition domain (HD) with a DNA-binding helix-turn-helix motif and an adjacent SIX domain, which may be involved in regulating protein-protein interactions (5). In addition to their critical functions during embryonic organogenesis, research studies suggest that SIX proteins play additional roles in postnatal cell cycle regulation, with potentially important implications in tumorigenesis (6,7).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through cell surface receptor tyrosine kinases. There are four members of the FGF receptor family: FGFR1 (flg), FGFR2 (bek, KGFR), FGFR3, and FGFR4. Each receptor contains an extracellular ligand binding domain, a transmembrane domain, and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR1 can be phosphorylated: Tyr463, 583, 585, 653, 654, 730, and 766. Tyr653 and Tyr654 are important for catalytic activity of activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCγ (4,5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through cell surface receptor tyrosine kinases. There are four members of the FGF receptor family: FGFR1 (flg), FGFR2 (bek, KGFR), FGFR3, and FGFR4. Each receptor contains an extracellular ligand binding domain, a transmembrane domain, and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR1 can be phosphorylated: Tyr463, 583, 585, 653, 654, 730, and 766. Tyr653 and Tyr654 are important for catalytic activity of activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCγ (4,5).