ek-7

Ephrin type-A receptor 5 (EphA5) expression was detected in all non-tumor gastric epithelia but was differentially expressed among gastric cancer samples. EphA5 is differentially expressed in gastric cancer. EphA5 may therefore be a potential therapeutic target and may have clinical utility as a marker for lymph node metastasis in gastric cancer. EPHA5 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 61.73 kDa and the accession number is A0A2K5W6J6.

Expression system: HEK293 Cells
Length: 27-412, Extracellular Domain
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-573, Partial
Activity: BLI、ELISA

Expression system: HEK293 Cells
Length: 1-573, Partial
Activity: BLI

Expression system: HEK293 Cells
Length: 1-556, Partial
Activity: ELISA

Expression system: Baculovirus Insect Cells
Length: 579-998, Partial
Activity: Enzyme activity

Enterokinase is a member of the trypsin family of serine proteases. The precursor protein is cleaved into two chains which then forms a heterodimer linked by a disulfide bond. The heavy chain anchors enterokinase in the intestinal brush border membrane and the light chain is the catalytic subunit, which initiates conversion activation of a subset of pancreatic proteolytic proenzymes. Enterokinase is the physiological activator of trypsinogen and has a specificity for the sequence (Asp)4-Lys-Ile. The mature trypsin in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases. In addition, Enterokinase is a tool protease widely utilized in the cleavage of recombinant fusion proteins.