EphB6 Antibody – Rat Monoclonal

Function: Kinase-defective receptor for members of the ephrin-B family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration by exerting both positive and negative effects upon stimulation with ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2 secretion and CD25 expression upon stimulation with ephrin-B2

By similarity.

Subunit structure: Interacts with CBL and EPHB1. Interacts with FYN; this interaction takes place in a ligand-independent manner

By similarity.

Subcellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted. Isoform 3: Secreted.

Tissue specificity: High level in thymus, and brain. Very low levels of expression in kidney, lung, liver, bone marrow, skeletal muscle, spleen from 2 week old and adult mice, heart, testes and embryonic stem cells. Ref.1

Domain: The protein kinase domain is predicted to be catalytically inactive. Its extracellular domain is capable of promoting cell adhesion and migration in response to low concentrations of ephrin-B2, but its cytoplasmic domain is essential for cell repulsion and inhibition of migration induced by high concentrations of ephrin-B2

By similarity.

Post-translational modification: Ligand-binding increases phosphorylation on tyrosine residues. Phosphorylation on tyrosine residues is mediated by transphosphorylation by the catalytically active EPHB1 in a ligand-independent manner. Tyrosine phosphorylation of the receptor may act as a switch on the functional transition from cell adhesion/attraction to de-adhesion/repulsion

By similarity.

Sequence similarities: Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.Contains 1 Eph LBD (Eph ligand-binding) domain.Contains 2 fibronectin type-III domains.Contains 1 protein kinase domain.Contains 1 SAM (sterile alpha motif) domain.