Analytical Data
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Gene name
Legumain
- Application
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Alternative Names
AEP; LGMN1; PRSC1; Protease,Cysteine 1; Asparaginyl endopeptidase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q99538
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Expression Region
Val18~Tyr433
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Molecular Weight
51kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Legumain, an asparaginyl endopeptidase, is a member of the cysteine protease family and has gained significant attention in the fields of biochemistry and molecular biology due to its unique substrate specificity and potential applications in therapeutic contexts. Its expression is primarily associated with various pathological conditions, including cancer, where it plays a role in tumor progression, immune evasion, and metastasis. Researchers have identified Legumain as a promising target for drug development, particularly in designing selective inhibitors that could combat tumors by modulating its activity. Additionally, Legumain is involved in the processing of several proteins, which further elucidates its importance in cellular functions and signaling pathways. The development of recombinant Legumain has facilitated detailed studies on its structure-function relationships, enabling researchers to unravel the mechanisms underlying its enzymatic activity and substrate interactions. This research not only enhances our understanding of Legumain's biological role but also contributes to the advancement of biotechnological applications, such as the creation of targeted drug delivery systems and diagnostic tools. With ongoing advancements in recombinant protein engineering, the characterization and manipulation of Legumain hold promise for innovative therapeutic strategies in cancer treatment and other diseases where this protease plays a critical role.











