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EPH-related receptor tyrosine kinase ligand 4 (Ephrin-A4) also known as EFNA4, is a member of the Ephrin family. The Eph family receptor interacting proteins (ephrins) are a family of proteins that serve as the ligands of the Eph receptor, which compose the largest known subfamily of receptor protein-tyrosine kinases (RTKs). Eph/ephrin interactions are implicated in axon guidance, neural crest cell migration, establishment of segmental boundaries, and formation of angiogenic capillary plexi. Ephrin subclasses are further distinguished by their mode of attachment to the plasma membrane: ephrin-A ligands bind EphA receptors and are anchored to the plasma membrane via a glycosylphosphatidylinositol (GPI) linkage, whereas ephrin-B ligands bind EphB receptors and are anchored via a transmembrane domain. An exception is the EphA4 receptor, which binds both subclasses of ephrins. Ephrin-A4/EFNA4 functions as a cell surface GPI-bound ligand for Eph receptor, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development.
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文献和实验Chromatin Interaction Analysis Using Paired‐End Tag Sequencing
Analysis using Paired?End Tag sequencing (ChIA?PET) is a technique developed for large?scale, de novo analysis of higher?order chromatin structures. Cells are treated with formaldehyde to cross?link chromatin interactions, DNA segments bound by protein
Purification of Human Multiprotein Complexes using OneSTrEP Technology
sufficient for visualising single protein bands by Coomassie Blue staining (Figure 1). The Strep -tag®II (SAWRHPQFGG) and its “double” sister, the One-STrEP-tag (tandem arrangement of Strep -tag®II, here called OneStrep), are reasonably small protein
Protein Chip for Detection of DNA Mutations
A large number of human genetic diseases, bacterial drug resistances, and single-nucleotide polymorphisms are caused by gene mutations. Rapid and high-throughput mutation detection methods are urgently demanded. A protein chip method
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