Measured by its ability to cleave a fluorogenic peptide substrate, Mca-YVADAPK(Dnp)-OH. The specific activity is >400 pmoles/min/μg. (Activation description: The proenzyme needs to be activated by Trypsin for an activated form)

Meprin alpha/MEP1A Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 69 kDa and the accession number is A0A0R4J043.

Mouse

HEK293 Cells

Meprin α/MEP1A,meprin A, α (PABA peptide hydrolase),meprin A, alpha (PABA peptide hydrolase),Mep-1a,Mep-1,Mep1,AW107200,AI098089

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. Predicted N terminal: Cys 21

> 95 % as determined by SDS-PAGE

Reconstituted with sterile deionized water to 0.25 mg/mL. Reconstitution conditions may vary depending on the lot.

It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.

Meprin A subunit alpha, also known as MEP1A, and Endopeptidase-2, is a single-pass type I membrane protein that 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, 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 the kidney and intestine. The multidomain alpha and beta subunits have high sequence identity. They have very different substrate specificities, oligomerization potentials, and are differentially regulated. Meprin A appears to be an important therapeutic target and urinary excretion appears to be a potential biomarker of acute kidney injury ( AKI ).