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Human Monoclonal LGMN Primary Antibody for ELISA - ABIN396827
Sowa, Bennett, Gygi, Harper: Defining the human deubiquitinating enzyme interaction landscape. in Cell 2009
Show all 5 references for ABIN396827
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 references for ABIN1881495
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
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
AEP promotes activation of the PI3K (show PIK3CA Antibodies)-AKT (show AKT1 Antibodies) 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 (show APP Antibodies) at N373 and N585 residues, selectively influencing the amyloidogenic fragmentation of APP (show APP Antibodies). 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.
legumain and TIMP-2 (show TIMP2 Antibodies) mRNAs were up-regulated in the endometrium during the luteal phase of the oestrous cycle and during early pregnancy
results suggest that legumain expression and activation and cleavage of annexin A2 (show ANXA2 Antibodies) are regulated by DJ-1 (show PARK7 Antibodies) through p53 (show TP53 Antibodies)
TDP-43 (show TARDBP Antibodies) is cleaved by AEP in brain.
TLR7 (show TLR7 Antibodies) 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 (show ICAM1 Antibodies)), and ras-related C3 botulinum toxin substrate 2 (RAC2 (show RAC2 Antibodies)), among others, in an invasive pre-B-cell line that produced leukemia in NOD-SCID (show PRKDC Antibodies) 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 (show EGFR Antibodies)
Immunohistochemical analyses revealed the expression of legumain in Iba1 (show AIF1 Antibodies)(+) microglial cells and glial fibrillary acidic protein (show GFAP Antibodies)-positive astrocytes of the peri (show POSTN Antibodies)-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 (show CST6 Antibodies) deficient mice.
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.
, asparaginyl endopeptidase
, protease, cysteine 1
, protease, cysteine, 1 (legumain)
, cysteine protease 1
, protease, cysteine, 1