Mouse Recombinant LCN2 protein, His Tag (V2LY-0526-LY8622)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Mouse
Tag
His Tag
Protein Construction
This product is Mouse Recombinant LCN2 protein, His Tag consist of Amino Acid: 1-200 and predicts a molecular mass of 22.3 kDa.
Molecule Mass
22.3 kDa
Verified
HPLC
Sequence
Amino Acid: 1-200
Species
Mouse

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

Purity
≥90% as determined by SDS-PAGE. ≥95% as determined by SEC-HPLC.
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
Lipocalin-2
Function
Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development (PubMed:12453413, PubMed:27780864, PubMed:20581821).
Binds iron through association with 2,3-dihydroxybenzoic acid (2,3-DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by association with an intracellular siderophore, iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration. Involved in apoptosis due to interleukin-3 (IL3) deprivation: iron-loaded form increases intracellular iron concentration without promoting apoptosis, while iron-free form decreases intracellular iron levels, inducing expression of the proapoptotic protein BCL2L11/BIM, resulting in apoptosis (By similarity).
Involved in innate immunity; limits bacterial proliferation by sequestering iron bound to microbial siderophores, such as enterobactin (PubMed:27780864).
Can also bind siderophores from M.tuberculosis (PubMed:15642259, PubMed:21978368).
Biological Process
Apoptotic processIEA:UniProtKB-KW
Defense response to bacteriumManual Assertion Based On ExperimentIDA:UniProtKB
Innate immune responseISS:UniProtKB
Positive regulation of cold-induced thermogenesisBy SimilarityISS:YuBioLab
Sequestering of iron ionManual Assertion Based On ExperimentIDA:UniProtKB
Siderophore transportISS:UniProtKB
Cellular Location
Secreted
Cytoplasmic granule lumen
Cytoplasmic vesicle lumen
Upon binding to the SLC22A17 (24p3R) receptor, it is internalized (By similarity).
Releases the bound iron in the acidic lumen of cytoplasmic vesicles (PubMed:12453413, PubMed:20581821).

Schröder, S. K., Gasterich, N., Weiskirchen, S., & Weiskirchen, R. (2023). Lipocalin 2 receptors: Facts, fictions, and myths. Frontiers in Immunology, 14.

Al Jaberi, S., Cohen, A., D’Souza, C., Abdulrazzaq, Y. M., Ojha, S., Bastaki, S., & Adeghate, E. A. (2021). Lipocalin-2: Structure, function, distribution and role in metabolic disorders. Biomedicine & Pharmacotherapy, 142, 112002.

Dekens, D. W., Eisel, U. L., Gouweleeuw, L., Schoemaker, R. G., De Deyn, P. P., & Naudé, P. J. (2021). Lipocalin 2 as a link between ageing, risk factor conditions and age-related brain diseases. Ageing Research Reviews, 70, 101414.

Petropoulou, P. I., Mosialou, I., Shikhel, S., Hao, L., Panitsas, K., Bisikirska, B., ... & Kousteni, S. (2020). Lipocalin-2 is an anorexigenic signal in primates. Elife, 9, e58949.

Santiago-Sánchez, G. S., Pita-Grisanti, V., Quiñones-Díaz, B., Gumpper, K., Cruz-Monserrate, Z., & Vivas-Mejía, P. E. (2020). Biological functions and therapeutic potential of lipocalin 2 in cancer. International journal of molecular sciences, 21(12), 4365.

Mosialou, I., Shikhel, S., Luo, N., Petropoulou, P. I., Panitsas, K., Bisikirska, B., ... & Kousteni, S. (2020). Lipocalin-2 counteracts metabolic dysregulation in obesity and diabetes. Journal of Experimental Medicine, 217(10), e20191261.

Bhusal, A., Rahman, M. H., Lee, W. H., Bae, Y. C., Lee, I. K., & Suk, K. (2019). Paradoxical role of lipocalin-2 in metabolic disorders and neurological complications. Biochemical Pharmacology, 169, 113626.

Hu, C., Yang, K., Li, M., Huang, W., Zhang, F., & Wang, H. (2018). Lipocalin 2: a potential therapeutic target for breast cancer metastasis. OncoTargets and therapy, 8099-8106.

Song, J., & Kim, O. Y. (2018). Perspectives in Lipocalin-2: emerging biomarker for medical diagnosis and prognosis for Alzheimer's disease. Clinical nutrition research, 7(1), 1-10.

Kang, S. S., Ren, Y., Liu, C. C., Kurti, A., Baker, K. E., Bu, G., ... & Fryer, J. D. (2018). Lipocalin-2 protects the brain during inflammatory conditions. Molecular psychiatry, 23(2), 344-350.

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

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