The Phospho-EphB1/EphB2 (Y594/604) Antibody (PACO06171) is a valuable tool for researchers studying the EphB1 and EphB2 proteins, key players in cell signaling pathways involved in cell growth, differentiation, and migration. This antibody, produced using high-quality materials and technology, specifically recognizes the phosphorylated forms of EphB1 and EphB2 at tyrosine residues 594 and 604.Phosphorylation of EphB1 and EphB2 at these specific sites is known to regulate their activity, affecting downstream signaling events that influence cellular processes such as cytoskeletal rearrangements and cell adhesion.
By targeting the phosphorylated forms of these proteins, researchers can gain insights into the molecular mechanisms underlying these biological functions.Validated for use in various experimental techniques such as Western blotting and immunofluorescence, the Phospho-EphB1/EphB2 (Y594/604) Antibody is a versatile tool for investigating the role of EphB receptors in development, cancer, and neurological disorders. Its high specificity and sensitivity make it an essential component of studies aiming to elucidate the intricate signaling networks governed by EphB1 and EphB2.
EphB1: a receptor tyrosine kinase of the Eph family. Receptor for members of the ephrin-B family: ephrin-B1, -B2 and -B3. The Eph receptor tyrosine kinase family, the largest in the tyrosine kinase group, has fourteen members. They bind membrane-anchored ligands, ephrins, at sites of cell-cell contact, regulating the repulsion and adhesion of cells that underlie the establishment, maintenance, and remodeling of patterns of cellular organization. Eph signals are particularly important in regulating cell adhesion and cell migration during development, axon guidance, homeostasis and disease. EphA receptors bind to GPI-anchored ephrin-A ligands, while EphB receptors bind to ephrin-B proteins that have a transmembrane and cytoplasmic domain. Interactions between EphB receptor kinases and ephrin-B proteins transduce signals bidirectionally, signaling to both interacting cell types. Eph receptors and ephrins also regulate the adhesion of endothelial cells and are required for the remodeling of blood vessels. The ligand-activated form of EphB1 interacts with GRB2, GRB10 and NCK through their respective SH2 domains. Four alternatively spliced isoforms are known.
UniProt Protein Details:
Protein type:Protein kinase, TK; Kinase, protein; EC 2.7.10.1; Protein kinase, tyrosine (receptor); Membrane protein, integral; TK group; Eph family
Chromosomal Location of Human Ortholog: 3q21-q23
Cellular Component: cytosol; early endosome membrane; extracellular region; integral to plasma membrane; plasma membrane
Biological Process: angiogenesis; axon guidance; cell-substrate adhesion; central nervous system projection neuron axonogenesis; detection of temperature stimulus involved in sensory perception of pain; ephrin receptor signaling pathway; establishment of cell polarity; neurogenesis; positive regulation of synaptogenesis; protein amino acid autophosphorylation; regulation of JNK cascade; retinal ganglion cell axon guidance
NCBI Summary:
Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The protein encoded by this gene is a receptor for ephrin-B family members. [provided by RefSeq, Jul 2008]