Mouse EphB1/Eph Receptor B1 (His & GST Tag) recombinant protein

Mouse EphB1/Eph Receptor B1 (His & GST Tag) recombinant protein

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Ephrin type-B receptor 1, also known as EphB1, 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 1

AW488255; CEK6; EPHT2; C130099E04RIK; ELKH; ELK; NET; FLJ37986; EPHB1; 9330129L11; HEK6; ENSMUSG00000074119

Q8CBF3

Ephb1

Baculovirus-Insect Cells

A DNA sequence encoding the cytoplasmic domain (Met 591-Ala 984) of mouse EPHB1 (Q8CBF3-1) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.

Mouse

The secreted recombinant mouse EPHB1/GST chimera consists of 631 amino acids and has a calculated molecular mass of 72.4 kDa. The recombinant protein migrates as an approximately 60 kDa band in SDS-PAGE under reducing conditions.

> 95 % as determined by SDS-PAGE

The specific activity was determined to be 234 nmol/min/mg using Poly(Glu,Tyr) 4:1 as substrate.