LGMN Mouse
Description
LGMN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 426 amino acids (18-435a.a.) and having a molecular mass of 48.6kDa. LGMN is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Produced in Sf9 Baculovirus cells, LGMN is a single, glycosylated polypeptide chain consisting of 426 amino acids (18-435a.a.) with a molecular weight of 48.6kDa. This protein is expressed with an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic methods.
Product Science Overview
Legumain is synthesized as an inactive zymogen and undergoes autocatalytic cleavage to become active. The active form of legumain has a molecular weight of approximately 49 kDa . It is characterized by its ability to cleave peptide bonds on the C-terminal side of asparagine residues, which is a unique feature among proteases.
- Protein Degradation: Legumain is involved in the degradation of intracellular proteins within lysosomes. It contributes to the turnover of proteins and the maintenance of cellular homeostasis.
- Antigen Presentation: In the immune system, legumain plays a role in the processing of antigens for presentation by major histocompatibility complex (MHC) class II molecules. This is essential for the activation of T cells and the initiation of immune responses.
- Extracellular Matrix Remodeling: Legumain is implicated in the remodeling of the extracellular matrix (ECM), which is important for tissue repair and regeneration. It has been shown to degrade ECM components, such as collagen, and is involved in processes like wound healing and fibrosis .
Recombinant mouse legumain is produced using genetic engineering techniques. The gene encoding mouse legumain is cloned and expressed in a suitable host system, such as a mouse myeloma cell line (NS0). The recombinant protein is then purified to high levels of purity, typically greater than 95% as determined by SDS-PAGE .
The recombinant form of legumain retains its enzymatic activity and is used in various research applications, including studies on protein degradation, antigen processing, and ECM remodeling. It is also utilized in drug discovery and development, particularly in the context of diseases where legumain activity is dysregulated, such as cancer and cardiovascular diseases .
- Cancer Research: Legumain is overexpressed in several types of cancer, and its activity is associated with tumor progression and metastasis. Inhibitors of legumain are being explored as potential therapeutic agents for cancer treatment.
- Cardiovascular Diseases: Elevated levels of legumain have been linked to adverse outcomes in cardiovascular diseases, such as acute myocardial infarction (AMI). Research has shown that legumain contributes to ECM degradation and cardiac remodeling post-AMI, making it a potential target for therapeutic intervention .
- Immunology: The role of legumain in antigen processing makes it a valuable tool for studying immune responses and developing vaccines. Recombinant legumain can be used to investigate the mechanisms of antigen presentation and T cell activation.
