EPH Receptor A2 Human Recombinant
EPH Receptor A2 Human Recombinant, sf9
EPH Receptor A3 Mouse Recombinant
HEK293 Cells.
EPH Receptor A4 Mouse Recombinant
EPH Receptor B1 Human Recombinant
Recombinantly produced in HEK293 cells, EPHB1 Human Recombinant is a single, glycosylated polypeptide chain. This protein consists of 529 amino acids (amino acids 18-540), resulting in a molecular weight of 59.2 kDa. It features a 6-amino acid His tag at the C-terminus and undergoes purification using proprietary chromatographic techniques.
EPH Receptor B2 Human Recombinant
EPH Receptor B4 Mouse Recombinant
Eph receptors, named after their expression in an erythropoietin-producing human hepatocellular carcinoma cell line, represent the largest family of receptor tyrosine kinases (RTKs) in the animal kingdom . They are divided into two subclasses, EphA and EphB, based on sequence similarity and their binding affinity for either the glycosylphosphatidylinositol (GPI)-linked ephrin-A ligands or the transmembrane-bound ephrin-B ligands . Humans express nine EphA receptors (EphA1-8 and EphA10) and five EphB receptors (EphB1-4 and EphB6) .
Eph receptors are widely expressed in various tissues and play crucial roles in numerous biological processes. They are involved in cell positioning, tissue patterning, and organ development . Eph receptors are expressed in most, if not all, cell types and are essential for cell contact-dependent communication . Their expression patterns and tissue distribution are highly regulated, with specific receptors being predominant in certain tissues .
Eph receptors are pivotal in regulating cell migration, adhesion, differentiation, and proliferation . They play significant roles in the development of the nervous system, cardiovascular system, and other organs . Eph/ephrin signaling is crucial for immune responses and pathogen recognition, influencing cell-cell communication and immune cell migration .
Eph receptors interact with their ligands, ephrins, on neighboring cells, leading to bidirectional signaling . This interaction can result in either cell-cell adhesion or repulsion, depending on the relative expression and affinity of the ligand-receptor pairs . The signaling cascades initiated by Eph/ephrin interactions involve autophosphorylation of tyrosine residues and recruitment of downstream signaling molecules .
The expression and activity of Eph receptors are tightly regulated at multiple levels. Transcriptional regulation, post-translational modifications, and interactions with other signaling pathways all contribute to the precise control of Eph receptor functions . Proteolytic cleavage and alternative splicing further increase the diversity and complexity of Eph receptor signaling .
Eph receptors have significant applications in biomedical research, diagnostic tools, and therapeutic strategies. They are potential targets for cancer therapy due to their roles in tumor progression, angiogenesis, and metastasis . Eph receptors are also being explored as targets for immunotherapy and as biomarkers for various diseases .
Eph receptors are involved in critical processes throughout the life cycle, from embryonic development to aging . During development, they regulate cell sorting, migration, and boundary formation . In adulthood, Eph receptors maintain tissue homeostasis and are implicated in neural plasticity and immune responses . Dysregulation of Eph signaling is associated with various diseases, including cancer and neurological disorders .