Recombinant Mouse Legumain Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-1621NP
BL-1621NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-1621NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Mouse Legumain Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-1621NP
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Product Overview

Description Recombinant Mouse Legumain/Asparaginyl Endopeptidase is produced by our Mammalian expression system and the target gene encoding Val18-Tyr435 is expressed with a 6His tag at the C-terminus.The enzyme achieves its activity under acidic pH.
Accession O89017
Synonym Legumain; Lgmn; Asparaginyl endopeptidase; Protease cysteine 1; Prsc1
Gene Background Mouse Legumain,also known as LGMN, is a cysteine protease belonging to peptidase family C13 and is expressed in kidney and placenta abundantly. LGMN has a strict specificity for hydrolysis of asparaginyl bonds. It can also cleave aspartyl bonds slowly, especially under acidic conditions. The mammalian legumain is involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system. It plays a role in the regulation of cell proliferation via its role in EGFR degradation. Legumain deficiency causes the accumulation of pro-Cathepsins B, H and L, another group of lysosomal cysteine proteases. Overexpression of Legumain in tumors is significant for invasion/metastasis. Mammalian legumain is inhibited by iodoacetamide and maleimides. Legumain activation appears to be autocatalytic and can be triggered by acidic pH.
Molecular Mass 48.7 KDa
Apmol Mass 60 KDa, reducing conditions
Formulation Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 20% Glycerol, pH 8.0.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution
Storage Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation.
Subcellular Location Lysosome.
Protein Families Peptidase C13 family
Database References
Tissue Specificity Detected in kidney proximal tubules (at protein level). Ubiquitous. Particularly abundant in kidney and placenta.

Gene Functions References

  1. Legumain regulates oxLDL-induced macrophage apoptosis by enhancing the autophagy pathway. PMID: 29414692
  2. Our data suggest that altered proteolytic activity of legumain in the bone microenvironment contributes to decreased bone mass in postmenopausal osteoporosis. PMID: 28162997
  3. This study showed that legumain may serve as a biomarker of disease, and that the occurrence of legumain-expressing macrophages in regions of acinar-to-ductal metaplasia suggests that this protease may influence reprogramming events that lead to inflammation-induced pancreatic cancer. PMID: 27514475
  4. AEP acts as a delta-secretase, cleaving APP at N373 and N585 residues, selectively influencing the amyloidogenic fragmentation of APP. AEP contributes to the age-dependent pathogenic mechanisms in Alzheimer disease. PMID: 26549211
  5. results suggest that legumain expression and activation and cleavage of annexin A2 are regulated by DJ-1 through p53 PMID: 26462467
  6. TDP-43 is cleaved by AEP in brain. PMID: 22718532
  7. TLR7 requires a proteolytic cleavage by AEP to generate a C-terminal fragment competent for signaling. PMID: 22916010
  8. We identified unique expression of asparaginyl endopeptidase (AEP), intercellular adhesion molecule 1 (ICAM1), and ras-related C3 botulinum toxin substrate 2 (RAC2), among others, in an invasive pre-B-cell line that produced leukemia in NOD-SCID mice PMID: 21606482
  9. AEP is required for normal protein catabolism by PTCs, and its loss induces proliferative and other abnormalities in the murine kidney, at least in part through defective regulation of the EGF receptor PMID: 21292981
  10. Immunohistochemical analyses revealed the expression of legumain in Iba1(+) microglial cells and glial fibrillary acidic protein-positive astrocytes of the peri-infarct area in mice after transient occlusion of the middle cerebral artery. PMID: 20234379
  11. AEP has a pivotal role in the endosomal/lysosomal degradation system PMID: 12775715
  12. unrestricted legumain activity is involved in disturbed epidermal cornification in cystatin M/E deficient mice. PMID: 15044380
  13. Lysosomal asparaginyl endopeptidase (AEP) is essential for processing of cathepsin L but not for class II major histocompatibility complex (MHC)-restricted antigen presentation. PMID: 15905550
  14. Legumain might have an important role in extracellular matrix remodeling via the degradation of fibronectin in renal proximal tubular cells. PMID: 17350006
  15. mutant mice lacking AEP develop fever, cytopenia, hepatosplenomegaly, and hemophagocytosis, extramedullary hematopoiesis in the spleen and abnormally enlarged histiocytes with ingested red blood cells in bone marrow. PMID: 19106291

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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