Mouse MEP1A Protein (His Tag)
AI098089,AW107200,Mep-1,Mep-1a,Mep1
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| Catalog Number | P50057-M08H |
|---|---|
| Organism Species | Mouse |
| Host | Human Cells |
| Synonyms | AI098089,AW107200,Mep-1,Mep-1a,Mep1 |
| Molecular Weight | The recombinant mouse MEP1A consists of 606 amino acids after removal of the signal peptide and has a predicted molecular mass of 69 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rm MEP1A is approximately 80-90 kDa due to glycosylation. |
| predicted N | Cys 21 |
| SDS-PAGE |  |
| Purity | > 95 % as determined by SDS-PAGE |
| 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. |
| Bio-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) |
| Research Area | Cancer |Signal transduction |Metabolism |Pathways and Processes |Metabolism processes |Apoptosis | |
| Formulation | Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
| Background | 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. 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 ). |
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