Recombinant Human Legumain (LGMN) Protein (His)

Name: Recombinant Human Legumain (LGMN) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02567P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Legumain (LGMN) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q99538
Target Symbol	LGMN
Synonyms	AEP; Asparaginyl endopeptidase; cysteine 1; Cysteine protease 1; EC 3.4.22.34; Legumain; LGMN; LGMN_HUMAN; LGMN1; Protease; Protease cysteine 1 (legumain); Protease cysteine 1; PRSC1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	VPIDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIVVMMYDDIAYSEDNPTPGIVINRPNGTDVYQGVPKDYTGEDVTPQNFLAVLRGDAEAVKGIGSGKVLKSGPQDHVFIYFTDHGSTGILVFPNEDLHVKDLNETIHYMYKHKMYRKMVFYIEACESGSMMNHLPDNINVYATTAANPRESSYACYYDEKRSTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKTISTMKVMQFQGMKRKASSPVPLPPVTHLDLTPSPDVPLTIMKRKLMNTN
Expression Range	18-323aa
Protein Length	Full Length of Mature Protein
Mol. Weight	38.8kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. 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. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system.
Subcellular Location	Lysosome.
Protein Families	Peptidase C13 family
Database References	HGNC: 9472 OMIM: 602620 KEGG: hsa:5641 STRING: 9606.ENSP00000334052 UniGene: PMID: 27993111 our results suggest that M2 tumour-associated macrophages affect degradation of the extracellular matrix and angiogenesis via overexpression of legumain, and therefore play an active role in the progression of DLBCL. PMID: 27464733 Legumain regulates oxLDL-induced macrophage apoptosis by enhancing the autophagy pathway. PMID: 29414692 MiRNA-3978 regulates peritoneal gastric cancer metastasis by targeting legumain expression, promoting cell migration/neoplasm invasiveness. PMID: 27793040 These results showed that Asparaginyl endopeptidase could promote invasion and metastasis by modulating epithelial-to-mesenchymal transition. PMID: 27102302 Our data suggest that altered proteolytic activity of legumain in the bone microenvironment contributes to decreased bone mass in postmenopausal osteoporosis. PMID: 28162997 Legumain is increased in both plasma and plaques of patients with carotid stenosis and might be a new and early biomarker of atherosclerosis. PMID: 27940038 Data suggest that melanoma cells internalize/absorb cystatin C from culture media, leading to increased intracellular cystatin C levels; cystatin E/M is internalized as well but at modest rate due to down-regulation of cell migration; however, the effect of intracellular cystatin E/M on down-regulation of legumain activity is pronounced. PMID: 28630039 AEP is activated and cleaves human alpha-synuclein at N103 in an age-dependent manner. PMID: 28671665 AEP promotes activation of the PI3K-AKT signaling pathway in prostate cancer cells. PMID: 27590439 upregulation of legumain is associated with malignant behavior of uveal melanoma. PMID: 26846877 Studies indicate that legumain, usually in lysosomes, is also found extracellularly and even translocates to the cytosol and the nucleus. PMID: 26403494 legumain might play an important role in cervical cancer cell migration and invasion. PMID: 26802645 Legumain appears to be involved in tumor development and deterioration. PMID: 26607955 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 High legumain expression is associated with breast cancer. PMID: 25605174 This unique feature was confirmed by the crystal structure of AEPpH4.5 (AEP was matured at pH 4.5 and crystallized at pH 8.5), in which the broken peptide bonds were religated and the structure was transformed back to its proenzyme form. PMID: 24407422 High legumain activity is associated with breast cancer. PMID: 24742492 AEP acts as a crucial mediator of tau-related clinical and neuropathological changes. PMID: 25326800 Identified an alternative oncogenic pathway for TRAF6 that uses AEP as its substrate. AEP and TRAF6 protein levels may have prognostic implications in breast cancer patients. Thus, AEP may serve as a biomarker as well as new therapeutic target PMID: 24610907 the relationship among Legumain expression, clinicopathologic, biological variables and patient prognosis in gastric carcinoma PMID: 24023813 HCT116 cells were transfected with p53 siRNA and the effect of knockdown of p53 expression on legumain expression was examined. The results showed that expression levels of both legumain mRNA and protein were decreased in the siRNA-treated cells. PMID: 23942113 Prostate cancer with a vesicular staining pattern of legumain had the potential of being highly invasive and aggressive in patients treated with radical prostatectomy. This suggests that legumain might contribute to the invasiveness and aggressiveness. PMID: 23124822 The multibranched and context-dependent activation process of legumain illustrates how proteases can act not only as signal transducers but as decision makers. PMID: 23776206 Involvement of brain acidosis in the etiopathogenesis of Alzheimer disease, and the asparaginyl endopeptidase-I2(PP2A)-protein phosphatase 2A-Tau hyperphosphorylation pathway. PMID: 23640887 glycosaminoglycans accelerated the autocatalytic activation of prolegumain PMID: 23160071 In the HCT116 and SW620 cell lines nuclear Data indicate that legumain was found to make up approximately 13% and 17% of the total legumain, respectively. PMID: 23326369 Data show a regulatory role of cystatin E/M in controlling both intra- and extracellular legumain activity. PMID: 22902879 TDP-43 is cleaved by AEP in brain. PMID: 22718532 Increased legumain expression was validated by real-time PCR and Western blots, correlated positively with an increased malignancy of ovarian tumors. PMID: 22441772 Accepting asparagines and, to lesser extent, aspartic acid in P1, super-activated legumain exhibits a marked pH dependence that is governed by the P1 residue of its substrate and conformationally stabilizing factors such as temperature or ligands PMID: 22232165 GARP is a key receptor controlling FOXP3 in T(reg) cells following T-cell activation in a positive feedback loop assisted by LGALS3 and LGMN PMID: 19453521 The Lgmn can serve as novel target in diabetes mellitus genetic therapy. PMID: 20536387 the level of cystatin E/M regulates legumain activity and hence the invasive potential of human melanoma cells PMID: 20074384 Legumain is expressed in both murine and human atherosclerotic lesions, may play a functional role in atherogenesis PMID: 18377911 human monocyte-derived dendritic cells harbor inactive proforms of AEP (legumain) that become activated upon maturation of dendritic cells with lipopolysaccharide PMID: 12860980 Freshly isolated human B lymphocytes lack significant asparagine-specific endoprotease (AEP/legumain) activity; cleavage by AEP is dispensable for proteolytic processing of myelin basic protein in this type of cell. PMID: 15100291 Increased legumain expression is associated with primary colorectal cancer PMID: 15788679 AEP may be a proteinases activated by acidosis triggering neuronal injury during neuroexcitotoxicity or ischemia. PMID: 18374643

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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.