LGMN Human

Legumain Human Recombinant
Cat. No.
BT3897
Source
Sf9, Baculovirus cells.
Synonyms
Legumain, PRSC1, Protease, Cysteine, 1 (Legumain), Asparaginyl Endopeptidase, Protease, Cysteine 1, EC 3.4.22.34, Cysteine Protease 1, LGMN1, AEP.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

LGMN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (18-433 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 422 amino acids and having a molecular mass of 48.4kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
LGMN is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Legumain, also known as LGMN, is a cysteine endopeptidase that exhibits strict specificity for hydrolyzing asparaginyl bonds. While it primarily targets asparaginyl bonds, LGMN can also cleave aspartyl bonds, albeit at a slower rate, particularly in acidic environments. This enzyme plays a critical role in the endosomal/lysosomal degradation pathway. Notably, Legumain deficiency leads to the accumulation of pro-cathepsins B, H, and L, which constitute another group of lysosomal cysteine proteases. Moreover, the overexpression of LGMN in tumors is implicated in invasion and metastasis.
Description
LGMN, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain encompassing amino acids 18 to 433. It is fused to a 6 amino acid His Tag at the C-terminus, resulting in a total of 422 amino acids and a molecular mass of 48.4 kDa. On SDS-PAGE, the molecular size will appear approximately between 40-57 kDa. The purification of LGMN is achieved through proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The LGMN protein solution is provided at a concentration of 1 mg/ml and is prepared in phosphate-buffered saline (pH 7.4) with 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For longer storage, it is recommended to freeze the product at -20°C. To further enhance long-term stability, adding a carrier protein (0.1% HSA or BSA) is advised. It's crucial to avoid repeated freeze-thaw cycles to maintain product integrity.
Purity
The purity of the LGMN protein is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
Legumain, PRSC1, Protease, Cysteine, 1 (Legumain), Asparaginyl Endopeptidase, Protease, Cysteine 1, EC 3.4.22.34, Cysteine Protease 1, LGMN1, AEP.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
VPIDDPEDGG KHWVVIVAGS NGWYNYRHQA DACHAYQIIH RNGIPDEQIV VMMYDDIAYS EDNPTPGIVI NRPNGTDVYQ GVPKDYTGED VTPQNFLAVL RGDAEAVKGI GSGKVLKSGP QDHVFIYFTD HGSTGILVFP NEDLHVKDLN ETIHYMYKHK MYRKMVFYIE ACESGSMMNH LPDNINVYAT TAANPRESSY ACYYDEKRST YLGDWYSVNW MEDSDVEDLT KETLHKQYHL VKSHTNTSHV MQYGNKTIST MKVMQFQGMK RKASSPVPLP PVTHLDLTPS PDVPLTIMKR KLMNTNDLEE SRQLTEEIQR HLDARHLIEK SVRKIVSLLA ASEAEVEQLL SERAPLTGHS CYPEALLHFR THCFNWHSPT YEYALRHLYV LVNLCEKPYP LHRIKLSMDH VCLGHYHHHH HH.

Product Science Overview

Discovery and Structure

Legumain was first discovered in beans and blood fluke (Schistosoma mansoni) before its mammalian version was described by Chen and co-workers in 1997 . Human legumain is synthesized as a 433 amino acid precursor with a signal peptide (residues 1-17). The proenzyme (residues 18-433) is expressed with an N-terminal His tag .

Function and Activity

Legumain plays a pivotal role in the degradation system of cells. Its activity is found in several tissues and is essential for the proper functioning of the lysosomal degradation pathway. The deficiency of legumain causes the accumulation of pro-cathepsins B, H, and L, which are other lysosomal cysteine proteases .

Legumain has anti-apoptotic effects in mammals and plays an antigen-presenting role in the inflammatory response. It can activate multiple signal pathways to promote cell apoptosis and migration, inflammatory response, and the development of atherosclerosis .

Recombinant Human Legumain

Recombinant human legumain is produced using a mouse myeloma cell line, NS0-derived human legumain/asparaginyl endopeptidase protein (Ile18-Tyr433), with an N-terminal 7-His tag . The recombinant form is used in various research applications, including studying its role in diseases and potential as a biomarker.

Applications and Research

Legumain is being studied for its potential as a biomarker for atherosclerosis due to its involvement in vascular remodeling, inflammatory response, plaque stability, and the degradation of the extracellular matrix . It is also being researched for its role in colorectal cancer and other diseases .

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Source
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