Human Recombinant LAP3 protein, His Tag (V2LY-0526-LY5252)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant LAP3 protein, His Tag consist of Amino Acid: 1-519 and predicts a molecular mass of 57.6 kDa.
Molecule Mass
57.6 kDa
Sequence
Amino Acid: 1-519
Species
Human

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

Purity
>90% as determined by SDS-PAGE.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
LAP3
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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