EphB2 Protein, Cynomolgus (HEK293, His)

The EphB2 protein is a receptor tyrosine kinase that binds to the transmembrane ephrin B ligand on adjacent cells to initiate bidirectional signaling. The forward signal originates from the receptor, while the reverse signal originates from the ephrin ligand. EphB2 Protein, Cynomolgus (HEK293, His) is the recombinant cynomolgus-derived EphB2 protein, expressed by HEK293 , with C-His labeled tag.

The EphB2 protein, a receptor tyrosine kinase, engages in promiscuous binding to transmembrane ephrin-B family ligands on adjacent cells, initiating contact-dependent bidirectional signaling. The downstream pathway originating from the receptor is known as forward signaling, while the signaling pathway downstream of the ephrin ligand is termed reverse signaling. EphB2 functions prominently in axon guidance during development, particularly in guiding commissural axons that form a major interhemispheric connection between the two temporal lobes of the cerebral cortex. Additionally, it is involved in guiding contralateral inner ear efferent growth cones at the midline and steering retinal ganglion cell axons to the optic disk. Beyond its role in axon guidance, EphB2 regulates the development and maturation of dendritic spines and stimulates the formation of excitatory synapses. Activation by EFNB1 abolishes ARHGEF15-mediated negative regulation on excitatory synapse formation. EphB2 controls various aspects of development, including angiogenesis, palate development, and inner ear development by regulating endolymph production. The EFNB2/EPHB2 complex, through both forward and reverse signaling, regulates the movement and adhesion of cells that tubularize the urethra and septate the cloaca. Moreover, EphB2 may function as a tumor suppressor and be involved in the regulation of platelet activation and blood coagulation.

Cynomolgus

HEK293

C-8*His

A0A7N9CQH5 (V19-P542)

/

Partial

VEETLMDSTTATAELGWMVHPPSGWEEVSGYDENMNTIRTYQVCNVFESSQNNWLRTKFIRRRGAHRIHVEMKFSVRDCSSIPSVPGSCKETFNLYYYEADFDSATKTFPNWMENPWVKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSRSGFYLAFQDYGGCMSLIAVRVFYRKCPRIIQNGAIFQETLSGAESTSLVAARGSCIANAEEVDVPIKLYCNGDGEWLVPIGRCMCKAGFEAVENGTVCRGCPSGTFKANQGDKACTHCPINSRTTSEGATNCVCRNGYYRADLDPLDMPCTTIPSAPQAVISSVNETSLMLEWTPPRDSGGREDLVYNIICKSCGSGRGACTRCGDNVQYAPRQLGLTEPRIYISDLLAHTQYTFEIQAVNGVTDQSPFSPQFASVNITTNQAAPSAVSIMHQVSRTVDSITLSWSQPDQPNGVILDYELQYYEKELSEYNATAIKSPTNTVTVQGLKAGAIYVFQVRARTVAGYGRYSGKMYFQTMTEAEYQTSIQEKLP

Approximately 65-75 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.