|Application ||WB, IHC-P, IF, E|
|Calculated MW||117493 Da|
|Antigen Region||1021-1050 aa|
|Other Names||Ephrin type-B receptor 2, Developmentally-regulated Eph-related tyrosine kinase, ELK-related tyrosine kinase, EPH tyrosine kinase 3, EPH-like kinase 5, EK5, hEK5, Renal carcinoma antigen NY-REN-47, Tyrosine-protein kinase TYRO5, Tyrosine-protein kinase receptor EPH-3, EPHB2, DRT, EPHT3, EPTH3, ERK, HEK5, TYRO5|
|Target/Specificity||This EphB2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1021-1050 amino acids from the C-terminal region of human EphB2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||EphB2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||DRT, EPHT3, EPTH3, ERK, HEK5, TYRO5|
|Function||Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Functions in axon guidance during development. Involved in the guidance of commissural axons, that form a major interhemispheric connection between the 2 temporal lobes of the cerebral cortex. Also involved in guidance of contralateral inner ear efferent growth cones at the midline and of retinal ganglion cell axons to the optic disk. In addition to axon guidance, also regulates dendritic spines development and maturation and stimulates the formation of excitatory synapses. Upon activation by EFNB1, abolishes the ARHGEF15-mediated negative regulation on excitatory synapse formation. Controls other aspects of development including angiogenesis, palate development and in inner ear development through regulation of endolymph production. Forward and reverse signaling through the EFNB2/EPHB2 complex regulate movement and adhesion of cells that tubularize the urethra and septate the cloaca. May function as a tumor suppressor.|
|Cellular Location||Cell membrane; Single-pass type I membrane protein. Cell projection, axon. Cell projection, dendrite|
|Tissue Location||Brain, heart, lung, kidney, placenta, pancreas, liver and skeletal muscle. Preferentially expressed in fetal brain|
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Provided below are standard protocols that you may find useful for product applications.
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 ligand-activated form of EphB2, which belongs to the Tyr family of protein kinases, interacts with multiple proteins, including GTPase-activating protein (RASGAP) through its SH2 domain. It binds RASGAP through the juxtamembrane tyrosines residues, and also interacts with PRKCABP and GRIP1 This type I membrane protein is expressed in brain, heart, lung, kidney, placenta, pancreas, liver and skeletal muscle. It is preferentially expressed in fetal brain. This protein contains putatively 2 fibronectin type III domains and 1 sterile alpha motif (SAM) domain.
Thanos, C.D., et al., Science 283(5403):833-836 (1999).
Tang, X.X., et al., Oncogene 17(4):521-526 (1998).
Fox, G.M., et al., Oncogene 10(5):897-905 (1995).
Ikegaki, N., et al., Hum. Mol. Genet. 4(11):2033-2045 (1995).
Iwase, T., et al., Biochem. Biophys. Res. Commun. 194(2):698-705 (1993).
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