Ephrin Type-B Receptor 1 (EPHB1) is a single-pass type I membrane protein that belongs to the Ephrin-B family of receptor tyrosine kinases that is involved in embryonic nervous and vascular system development. EPHB1 EPHT2 contains two fibronectin type-III domains, one protein kinase domain and one SAM (sterile α motif) domain. EPHB1 could stimulate fibroblast motility on extracellular matrix in a kinase-dependent manner, which also correlated with its association with Grb7, an adaptor molecule implicated in the regulation of cell migration. It binds to ephrin-B1, ephrin-B2 and ephrin-B3. EPHB1 plays an important roles in diverse biological processes including nervous system development, angiogenesis, and neural synapsis formation and maturation and may be involved in cell-cell interactions in the nervous system.
MKK6 Protein, Human, Recombinant is expressed in Baculovirus insect cells. The predicted molecular weight is 37.6 kDa and the accession number is A8K3Y2.
EphB1 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 60 kDa and the accession number is P54762-1.
EphB1 Protein, Human, Recombinant (aa 565-984, His & GST) is expressed in Baculovirus insect cells with His and GST tag. The predicted molecular weight is 75.3 kDa and the accession number is AAI11745.1.
Enterokinase (EK) is a duodenal protease involved in digestion by activating trypsinogen into trypsin, which in turn activates other pancreatic enzymes. EK specifically cleaves after the sequence Asp-Asp-Asp-Asp-Lys (DDDDK↓) and is inactive if a proline follows the site. Recombinant bovine enterokinase (rbEK) shows higher activity than EK from other species and is widely used in biochemical applications. It is a glycosylated single-chain protein of ~200 amino acids, tagged with C-terminal 6×His for Ni²⁺ affinity purification and easy removal after digestion. The purified rbEK has a molecular weight of ~40 kDa and is fully biologically active.
Enterokinase (EK) is a serine protease produced in the duodenum and involved in mammalian digestion. It activates trypsinogen to trypsin, thereby indirectly initiating the activation of pancreatic digestive enzymes. EK specifically cleaves after the recognition sequence Asp-Asp-Asp-Asp-Lys, but is inactive if a proline follows the cleavage site. This recombinant bovine enterokinase is the light chain catalytic subunit, comprising a single glycosylated polypeptide chain corresponding to residues Ile801–His1035 of the native protein (Accession # P98072). Expressed in Pichia pastoris under animal-free conditions, the enzyme is highly active and suitable for applications in drug and vaccine development. A C-terminal 6×His tag is included to allow efficient removal by Ni²⁺ affinity chromatography following cleavage reactions.
Although EphB3 expression is down-regulated in colorectal cancer (CRC) cells compared with normal intestinal epithelial cells.EphB3 is down-regulated in CRC compared to normal mucosa. Hypermethylation of CpG island is contributed to downregulation of EphB3 in CRC. EphB3 expression in tumor cells may be a useful prognostic indicator for patients with CRC.