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Mouse Anti-LAP3 Recombinant Antibody (4G10) (CBMAB-L0688-YJ)

Provided herein is a Mouse monoclonal antibody, which binds to Leucine Aminopeptidase 3 (LAP3). The antibody can be used for immunoassay techniques, such as ELISA, WB.
See all LAP3 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
4G10
Antibody Isotype
IgG2a, κ
Application
ELISA, WB

Basic Information

Immunogen
Partial recombinant protein corresponding to aa 420-519 from human LAP3 with GST tag. MW of the GST tag alone is 26kD.
Specificity
Human
Antibody Isotype
IgG2a, 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!]

Buffer
PBS, pH 7.2
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
aa 420-519

Target

Full Name
LAP3
Introduction
Diseases associated with LAP3 include Trichomoniasis and Bacterial Vaginosis. Among its related pathways are Arginine and proline metabolism and Metabolism. Gene Ontology (GO) annotations related to this gene include aminopeptidase activity and peptidase activity. An important paralog of this gene is NPEPL1. LAP3 is presumably involved in the processing and regular turnover of intracellular proteins. LAP3 catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Entrez Gene ID
51056
UniProt ID
P28838
Alternative Names
HEL-S-106; LAP; LAPEP; PEPS
Function
Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates. Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status.
Biological Process
Proteolysis1 PublicationNAS:UniProtKB
Cellular Location
Cytoplasm

Feng, L., Riaz, F., Lu, K., Cheng, X., Chen, Y., Zhao, R., ... & Li, D. (2023). Leucine aminopeptidase 3: a promising serum biomarker candidate for nonalcoholic steatohepatitis diagnosis. International Immunopharmacology, 119, 110152.

Osana, S., Kitajima, Y., Naoki, S., Murayama, K., Takada, H., Tabuchi, A., ... & Nagatomi, R. (2023). The aminopeptidase LAP3 suppression accelerates myogenic differentiation via the AKT‐TFE3 pathway in C2C12 myoblasts. Journal of Cellular Physiology, 238(9), 2103-2119.

Ge, L., Su, P., Wang, S., Gu, Y., Cao, X., Lv, X., ... & Sun, W. (2022). New insight into the role of the leucine aminopeptidase 3 (Lap3) in cell proliferation and myogenic differentiation in sheep embryonic myoblasts. Genes, 13(8), 1438.

Feng, L., Chen, Y., Xu, K., Li, Y., Riaz, F., Lu, K., ... & Li, D. (2022). Cholesterol-induced leucine aminopeptidase 3 (LAP3) upregulation inhibits cell autophagy in pathogenesis of NAFLD. Aging (Albany NY), 14(7), 3259.

Kuhara, K., Kitagawa, T., Baron, B., Tokuda, K., Sakamoto, K., Nagano, H., ... & Kuramitsu, Y. (2021). Proteomic analysis of hepatocellular carcinoma tissues with encapsulation shows up-regulation of leucine aminopeptidase 3 and phosphoenolpyruvate carboxykinase 2. Cancer Genomics & Proteomics, 18(3), 307-316.

Skoczynska, A., Skoczynska, M., Wojakowska, A., Turczyn, B., Gruszczynski, L., & Scieszka, M. (2021). Urinary leucine aminopeptidase 3 in population environmentally exposed to airborne arsenic. Human & Experimental Toxicology, 40(8), 1308-1319.

Wang, X., Ji, S., Ma, Y., Xing, X., Zhou, Y., Xu, X., ... & Fang, C. (2020). Vimentin plays an important role in the promotion of breast cancer cell migration and invasion by leucine aminopeptidase 3. Cytotechnology, 72, 639-647.

Yang, H., Dai, G., Wang, S., Zhao, Y., Wang, X., Zhao, X., ... & Fang, C. (2020). Inhibition of the proliferation, migration, and invasion of human breast cancer cells by leucine aminopeptidase 3 inhibitors derived from natural marine products. Anti-Cancer Drugs, 31(1), 60-66.

Fang, C., Zhang, J., Yang, H., Peng, L., Wang, K., Wang, Y., ... & Wang, X. (2019). Leucine aminopeptidase 3 promotes migration and invasion of breast cancer cells through upregulation of fascin and matrix metalloproteinases‐2/9 expression. Journal of Cellular Biochemistry, 120(3), 3611-3620.

Wu, H., Jiang, W., Li, B., Yang, H., Zhao, X., Zhang, H., ... & Fang, C. (2019). A new method to evaluate the enzyme-suppressing activity of a leucine aminopeptidase 3 inhibitor. Drug Discoveries & Therapeutics, 13(1), 17-21.

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

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We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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