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Mouse Anti-LGMN Recombinant Antibody (M1) (CBMAB-A4943-LY)

The product is antibody recognizes LGMN. The antibody M1 immunoassay techniques such as: sELISA, ELISA.
See all LGMN antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
M1
Antibody Isotype
IgG1, κ
Application
sELISA, ELISA

Basic Information

Immunogen
LGMN (AAH03061.1, 1 a.a. ~ 433 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
LGMN
Introduction
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. [provided by RefSeq]
Entrez Gene ID
5641
UniProt ID
Q99538
Alternative Names
AEP; LGMN1; PRSC1
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 (By similarity).
May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system.
Biological Process
Activation of cysteine-type endopeptidase activityManual Assertion Based On ExperimentIDA:ARUK-UCL
Antigen processing and presentation of exogenous peptide antigen via MHC class IITAS:Reactome
Associative learningBy SimilarityISS:ARUK-UCL
Cellular response to amyloid-betaManual Assertion Based On ExperimentIDA:ARUK-UCL
Cellular response to calcium ionManual Assertion Based On ExperimentIDA:ARUK-UCL
Cellular response to hepatocyte growth factor stimulusManual Assertion Based On ExperimentIDA:ARUK-UCL
Dendritic spine organizationBy SimilarityISS:ARUK-UCL
MemoryBy SimilarityISS:ARUK-UCL
Negative regulation of ERBB signaling pathwayISS:UniProtKB
Negative regulation of gene expressionManual Assertion Based On ExperimentIMP:ARUK-UCL
Negative regulation of multicellular organism growthIEA:Ensembl
Negative regulation of neuron apoptotic processManual Assertion Based On ExperimentIGI:MGI
Positive regulation of cell population proliferationManual Assertion Based On ExperimentIMP:ARUK-UCL
Positive regulation of endothelial cell chemotaxisManual Assertion Based On ExperimentIDA:ARUK-UCL
Positive regulation of long-term synaptic potentiationBy SimilarityISS:ARUK-UCL
Positive regulation of mitotic cell cycleManual Assertion Based On ExperimentIMP:ARUK-UCL
Positive regulation of monocyte chemotaxisManual Assertion Based On ExperimentIDA:ARUK-UCL
ProteolysisBy SimilarityISS:UniProtKB
Proteolysis involved in cellular protein catabolic processISS:UniProtKB
Receptor catabolic processISS:UniProtKB
Renal system processISS:UniProtKB
Response to acidic pHManual Assertion Based On ExperimentIDA:ARUK-UCL
Self proteolysisManual Assertion Based On ExperimentIDA:ARUK-UCL
Vacuolar protein processingManual Assertion Based On ExperimentIBA:GO_Central
Vitamin D metabolic processTAS:Reactome
Cellular Location
Lysosome
PTM
Glycosylated.
Activated by autocatalytic processing at pH 4.

Ke, B. Y., Qin, Y. S., Cheng, L., & Wang, S. Z. (2023). Legumain: a potential biomarker for atherosclerosis. Journal of Pharmacy and Pharmacology, 75(11), 1395-1404.

Ehsan, M., Hu, R. S., Wang, M., Hou, J. L., Rashid, M., & Malik, M. I. (2023). Immune modulation of goat monocytes by Fasciola gigantica Legumain-1 protein (Fg-LGMN-1). Experimental Parasitology, 108671.

He, Y., Zou, P., Lu, J., Lu, Y., Yuan, S., Zheng, X., ... & Zhou, S. (2023). CD4+ T-Cell Legumain Deficiency Attenuates Hypertensive Damage via Preservation of TRAF6. Circulation Research.

Pan, L., Bai, P., Weng, X., Liu, J., Chen, Y., Chen, S., ... & Ge, J. (2022). Legumain is an endogenous modulator of integrin αvβ3 triggering vascular degeneration, dissection, and rupture. Circulation, 145(9), 659-674.

Liu, C., Wang, J., Zheng, Y., Zhu, Y., Zhou, Z., Liu, Z., ... & Chen, J. (2022). Autocrine pro-legumain promotes breast cancer metastasis via binding to integrin αvβ3. Oncogene, 41(34), 4091-4103.

Jia, D., Chen, S., Bai, P., Luo, C., Liu, J., Sun, A., & Ge, J. (2022). Cardiac resident macrophage-derived legumain improves cardiac repair by promoting clearance and degradation of apoptotic cardiomyocytes after myocardial infarction. Circulation, 145(20), 1542-1556.

Reddy, B. D., Beeraka, N. M., Chitturi, C. H., & Madhunapantula, S. V. (2021). An overview of targeting legumain for inhibiting cancers. Current Pharmaceutical Design, 27(31), 3337-3348.

Wang, H., Chen, B., Lin, Y., Zhou, Y., & Li, X. (2020). Legumain promotes gastric cancer progression through tumor-associated macrophages in vitro and in vivo. International Journal of Biological Sciences, 16(1), 172.

Ren, Y. C., Zhao, Q., He, Y., Li, B., Wu, Z., Dai, J., ... & Hu, G. (2020). Legumain promotes fibrogenesis in chronic pancreatitis via activation of transforming growth factor β1. Journal of Molecular Medicine, 98, 863-874.

Wang, Y., Zhang, S., Wang, H., Cui, Y., Wang, Z., Cheng, X., ... & Liu, T. (2020). High level of legumain was correlated with worse prognosis and peritoneal metastasis in gastric cancer patients. Frontiers in Oncology, 10, 966.

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For research use only. Not intended for any clinical use.

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