MEP1A Protein (His tag) (recombinant mouse)

Activity: Measured by its ability to cleave a fluorogenic peptide substrate, Mca-YVADAPK(Dnp)-OH, R&D Systems, Catalog # ES007.The specific activity is >400 pmoles/min/µg.(Activation description: The proenzyme needs to be activated by Trypsin for an activated form) Protein Construction: A DNA sequence encoding the mouse MEP1A (NP_032611.2) (Met 1-Arg 615) was expressed, fused with a polyhistidine tag at the C-terminus. Sequence: Met 1-Arg 615. Fusion tag: C-His Endotoxin: < 1.0 EU per µg of the protein as determined by the LAL method. Apparent Molecular Mass: 80-90 kDa. Protein function: Meprin A subunit alpha, also known as MEP1A, and Endopeptidase-2, is a single-pass type I  membrane protein which belongs to the peptidase M12A family. MEP1A contains one EGF-like domain, one MAM domain, and one MATH domain. Meprins are unique plasma membrane and secreted metalloproteinases that are highly regulated at the transcriptional and post-translational levels. Meprin alpha and beta subunits are abundantly expressed in kidney and intestinal epithelial cells, are secreted into the urinary tract and intestinal lumen, and are found in leukocytes and cancer cells under certain conditions. Meprins are capable of proteolytically degrading extracellular matrix proteins, proteolytically processing bioactive proteins, and play a role in inflammatory processes. Meprin A and B are highly regulated, secreted and cell-surface homo- and hetero-oligomeric enzymes. Meprins are abundantly expressed in kidney and intestine. The multidomain alpha and beta subunits have high sequence identity. T