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Specificity
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Ab10612 recognizes recombinant mouse and rat EphA5 and a customer reported no signal in mouse brain lysate. Therefore it appears the antibody is not suitable for detection of endogenous EphA5.
The antibody shows approximately 15% cross-reactivity with recombinant mouse EphA3, recombinant mouse EphA4, recombinant mouse EphA6, recombinant mouse EphB7, recombinant mouse EphA8, and recombinant rat EphB1.
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Relevance
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EphA5, also known as Ehk1, Bsk, Cek7, Hek7, and Rek7, is a member of the Eph receptor family, which binds members of the Ephrin ligand family. Two classes of receptors exist, designated A and B, that have an extracellular domain made up of a globular domain, a cysteine-rich domain, and two fibronectin type III domains, followed by the transmembrane region and cytoplasmic region. The cytoplasmic region is a juxtamembrane region with two tyrosines, the major autophosphorylation sites, along with a kinase domain, and a conserved sterile alpha motif (SAM) in the C-terminus, the latter including one conserved tyrosine.
The extracellular domains of rat and mouse EphA5 share approximately 98.5% amino acid identity. Rat EphA5 shares 96.5% amino acid homology with human EphA5. The calculated molecular mass of the reduced rat EphA5/Fc monomer is approximately 84 kDa, but as a result of glycosylation, recombinant EphA5/Fc migrates as an approximately 110 kDa protein under reducing conditions in SDS-PAGE. Ligand recognition and binding leads to kinase activation of the intrinsic kinase activity. EphA5 binds to Ephrin A1, Ephrin A2, Ephrin A3, Ephrin A4 and Ephrin A5. Only membrane-bound or Fc-clustered ligands have been shown to activate the receptor in vitro. Soluble monomeric ligands bind the receptor, but do not induce receptor autophosphorylation and activation. The ephrin ligands and Eph receptors display reciprocal expression in vivo. Developing and adult neural tissue express nearly all of the Eph receptors and ephrin ligands. Ephs and ephrins play a significant role in angiogenesis.
EphA5, also known as Ehk1, Bsk, Cek7, Hek7, and Rek7, is a member of the Eph receptor family, which binds members of the Ephrin ligand family. Two classes of receptors exist, designated A and B, that have an extracellular domain made up of a globular domain, a cysteine-rich domain, and two fibronectin type III domains, followed by the transmembrane region and cytoplasmic region. The cytoplasmic region is a juxtamembrane region with two tyrosines, the major autophosphorylation sites, along with a kinase domain, and a conserved sterile alpha motif (SAM) in the C-terminus, the latter including one conserved tyrosine.
The extracellular domains of rat and mouse EphA5 share approximately 98.5% amino acid identity. Rat EphA5 shares 96.5% amino acid homology with human EphA5. The calculated molecular mass of the reduced rat EphA5/Fc monomer is approximately 84 kDa, but as a result of glycosylation, recombinant EphA5/Fc migrates as an approximately 110 kDa protein under reducing conditions in SDS-PAGE. Ligand recognition and binding leads to kinase activation of the intrinsic kinase activity. EphA5 binds to Ephrin A1, Ephrin A2, Ephrin A3, Ephrin A4 and Ephrin A5. Only membrane-bound or Fc-clustered ligands have been shown to activate the receptor in vitro. Soluble monomeric ligands bind the receptor, but do not induce receptor autophosphorylation and activation. The ephrin ligands and Eph receptors display reciprocal expression in vivo. Developing and adult neural tissue express nearly all of the Eph receptors and ephrin ligands. Ephs and ephrins play a significant role in angiogenesis.
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