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Human Polyclonal LGMN Primary Antibody for WB - ABIN1881495
Clerin, Shih, Deng, Hebert, Resmini, Shields, Feldman, Winkler, Albert, Maganti, Wong, Paulsen, Keith, Vlasuk, Pittman: Expression of the cysteine protease legumain in vascular lesions and functional implications in atherogenesis. in Atherosclerosis 2009
Show all 3 Pubmed References
Human Monoclonal LGMN Primary Antibody for ELISA - ABIN562455
Liu, Bajjuri, Liu, Sinha: Targeting cell surface alpha(v)beta(3) integrin increases therapeutic efficacies of a legumain protease-activated auristatin prodrug. in Molecular pharmaceutics 2012
Human Polyclonal LGMN Primary Antibody for WB - ABIN519319
Garcia-Cattaneo, Gobert, Müller, Toscano, Flores, Lescure, Del Nery, Benaroch: Cleavage of Toll-like receptor 3 by cathepsins B and H is essential for signaling. in Proceedings of the National Academy of Sciences of the United States of America 2012
Studies identified Legumain (LGMN) as a new target which is highly expressed in the tumor microenvironment and in tumor cells. [review]
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.
Legumain regulates oxLDL-induced macrophage apoptosis by enhancing the autophagy pathway.
MiRNA-3978 regulates peritoneal gastric cancer metastasis by targeting legumain expression, promoting cell migration/neoplasm invasiveness.
These results showed that Asparaginyl endopeptidase could promote invasion and metastasis by modulating epithelial-to-mesenchymal transition.
Our data suggest that altered proteolytic activity of legumain in the bone microenvironment contributes to decreased bone mass in postmenopausal osteoporosis.
Legumain is increased in both plasma and plaques of patients with carotid stenosis and might be a new and early biomarker of atherosclerosis.
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.
AEP is activated and cleaves human alpha-synuclein at N103 in an age-dependent manner.
AEP promotes activation of the PI3K-AKT signaling pathway in prostate cancer cells.
upregulation of legumain is associated with malignant behavior of uveal melanoma.
Studies indicate that legumain, usually in lysosomes, is also found extracellularly and even translocates to the cytosol and the nucleus.
legumain might play an important role in cervical cancer cell migration and invasion.
Legumain appears to be involved in tumor development and deterioration.
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.
High legumain expression is associated with breast cancer.
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.
High legumain activity is associated with breast cancer.
AEP acts as a crucial mediator of tau-related clinical and neuropathological changes.
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
findings thus support that AEP-mediated cleavage of alpha-Syn at N103 is required for the association and activation of MAO-B, mediating Parkinson's disease pathogenesis.
This study showed that legumain may serve as a biomarker of disease, and that the occurrence of legumain-expressing macrophages in regions of acinar-to-ductal metaplasia suggests that this protease may influence reprogramming events that lead to inflammation-induced pancreatic cancer.
results suggest that legumain expression and activation and cleavage of annexin A2 are regulated by DJ-1 through p53
TDP-43 is cleaved by AEP in brain.
TLR7 requires a proteolytic cleavage by AEP to generate a C-terminal fragment competent for signaling.
We identified unique expression of asparaginyl endopeptidase (AEP), intercellular adhesion molecule 1 (ICAM1), and ras-related C3 botulinum toxin substrate 2 (RAC2), among others, in an invasive pre-B-cell line that produced leukemia in NOD-SCID mice
AEP is required for normal protein catabolism by PTCs, and its loss induces proliferative and other abnormalities in the murine kidney, at least in part through defective regulation of the EGF receptor
Immunohistochemical analyses revealed the expression of legumain in Iba1(+) microglial cells and glial fibrillary acidic protein-positive astrocytes of the peri-infarct area in mice after transient occlusion of the middle cerebral artery.
AEP has a pivotal role in the endosomal/lysosomal degradation system
unrestricted legumain activity is involved in disturbed epidermal cornification in cystatin M/E deficient mice.
Lysosomal asparaginyl endopeptidase (AEP) is essential for processing of cathepsin L but not for class II major histocompatibility complex (MHC)-restricted antigen presentation.
Legumain might have an important role in extracellular matrix remodeling via the degradation of fibronectin in renal proximal tubular cells.
mutant mice lacking AEP develop fever, cytopenia, hepatosplenomegaly, and hemophagocytosis, extramedullary hematopoiesis in the spleen and abnormally enlarged histiocytes with ingested red blood cells in bone marrow.
legumain and TIMP-2 mRNAs were up-regulated in the endometrium during the luteal phase of the oestrous cycle and during early pregnancy
at the early stage of seed development, deltaVPE is involved in cell death of limited cell layers, the purpose of which is to form a seed coat
The LGMN and CST6 system at the maternal-fetal interface may play an important role in the establishment and maintenance of pregnancy in pigs.
This gene encodes a cysteine protease that has a strict specificity for hydrolysis of asparaginyl bonds. This enzyme may be involved in the processing of bacterial peptides and endogenous proteins for MHC class II presentation in the lysosomal/endosomal systems. Enzyme activation is triggered by acidic pH and appears to be autocatalytic. Protein expression occurs after monocytes differentiate into dendritic cells. A fully mature, active enzyme is produced following lipopolysaccharide expression in mature dendritic cells. Overexpression of this gene may be associated with the majority of solid tumor types. This gene has a pseudogene on chromosome 13. Several alternatively spliced transcript variants have been described, but the biological validity of only two has been determined. These two variants encode the same isoform.
, cysteine protease 1
, protease, cysteine 1
, protease, cysteine, 1 (legumain)
, protease, cysteine, 1