Human EphB2/Eph Receptor B2 (His & Fc Tag) recombinant protein

Human EphB2/Eph Receptor B2 (His & Fc Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

Ephrin type-B receptor 2, also known as EphB2, belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family which 16 known receptors (14 found in mammals) are involved: EPHA1, EPHA2, EPHA3, EPHA4, EPHA5, EPHA6, EPHA7, EPHA8, EPHA9, EPHA10, EPHB1, EPHB2, EPHB3, EPHB4, EPHB5, EPHB6. EphB2 receptor tyrosine kinase phosphorylates syndecan-2 and that this phosphorylation event is crucial for syndecan-2 clustering and spine formation. The Eph family of receptor tyrosine kinases (comprising EphA and EphB receptors) has been implicated in synapse formation and the regulation of synaptic function and plasticity6. Ephrin receptors are components of cell signalling pathways involved in animal growth and development, forming the largest sub-family of receptor tyrosine kinases (RTKs). Ligand-mediated activation of Ephs induce various important downstream effects and Eph receptors have been studied for their potential roles in the development of cancer. EphB receptor tyrosine kinases are enriched at synapses, suggesting that these receptors play a role in synapse formation or function. We find that EphrinB binding to EphB induces a direct interaction of EphB with NMDA-type glutamate receptors. This interaction occurs at the cell surface and is mediated by the extracellular regions of the two receptors, but does not require the kinase activity of EphB.

Ephrin type-B receptor 2

CAPB; DRT; ERK; SEK3; ETECK; NUK; EPHT3; QEK5; CEK5; PCBC; EPHB2; TYRO5; HEK5; RP23-426N4.7; EK5; PRKM5; MGC87492

Q6NVW1

EPHB2; DRT; EPHT3; EPTH3; ERK; HEK5; TYRO5

Human Cells

A DNA sequence encoding the extracellular domain (Met 1-Leu 543) of human EphB2 (NP_059145.2) was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus.

Human

The recombinant human EphB2/Fc is a disulfide-linked homodimer. The reduced monomer consists of 773 amino acids and has a predicted molecular mass of 86 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh EphB2/Fc monomer is approximately 90-100 kDa due to glycosylation.

> 90 % as determined by SDS-PAGE

Measured by its ability to bind recombinant human EphrinB2 in a functional ELISA.