Analytical Data
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Gene name
LGMN
- Application
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Alternative Names
LGMN;PRSC1;Legumain
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99538
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Expression Region
18-323aa
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AA Sequence
VPIDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIVVMMYDDIAYSEDNPTPGIVINRPNGTDVYQGVPKDYTGEDVTPQNFLAVLRGDAEAVKGIGSGKVLKSGPQDHVFIYFTDHGSTGILVFPNEDLHVKDLNETIHYMYKHKMYRKMVFYIEACESGSMMNHLPDNINVYATTAANPRESSYACYYDEKRSTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKTISTMKVMQFQGMKRKASSPVPLPPVTHLDLTPSPDVPLTIMKRKLMNTN
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Molecular Weight
38.8kDa
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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
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Protein Description
LGMN, or Legumain, is a cysteine protease that plays a crucial role in various physiological and pathological processes, including apoptosis, immune response, and cancer progression. Its unique substrate specificity for asparaginyl and aspartic acid residues makes LGMN a valuable target for therapeutic interventions. Researchers have shown that LGMN is significantly upregulated in several cancer types, making it a promising biomarker and potential target for cancer immunotherapy. The study of LGMN recombinant proteins is instrumental in elucidating its biological functions, mechanisms of action, and potential applications in drug development. Advances in recombinant DNA technology have facilitated the production of LGMN proteins for structural and functional studies, which are essential for understanding how this protease modulates various cellular processes. By creating specific inhibitors or biologics that target LGMN, researchers aim to develop novel strategies for cancer treatment and improve patient outcomes. Furthermore, LGMN's involvement in extracellular matrix remodeling and its role in inflammation highlight its significance beyond cancer, emphasizing the need for comprehensive studies on its diverse biological activities. As research progresses, LGMN continues to emerge as a critical focus in the fields of cancer biology, immunology, and therapeutic design.
