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Mouse Anti-LAP3 Recombinant Antibody (A867) (CBMAB-AP11359LY)

The product is antibody recognizes LAP3. The antibody A867 immunoassay techniques such as: ELISA, IHC, WB.
See all LAP3 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
A867
Antibody Isotype
IgG1
Application
ELISA, IHC, WB

Basic Information

Immunogen
Fusion Protein of LAP3
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1
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
Affinity purity
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
LAP3
Entrez Gene ID
Human51056
Mouse66988
Rat289668
UniProt ID
HumanP28838
MouseQ9CPY7
RatQ68FS4
Alternative Names
Cytosol aminopeptidase,LAP,LAP 3,LAP3,LAPEP,leucine aminopeptidase 3,Leucyl aminopeptidase,PEPS,Peptidase S,Proline aminopeptidase,Prolyl aminopeptidase
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.

Custom Antibody Labeling

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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