Mouse Anti-LCN2 Recombinant Antibody (697) (CBMAB-L0847-YJ)

Name: Mouse Anti-LCN2 Recombinant Antibody (697)
SKU: CBMAB-L0847-YJ
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

697

Application

Specificity

Human

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!]

Buffer

PBS, 0.1% BSA

Preservative

0.02% Sodium Azide

Storage

Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

More Infomation

Target

Full Name

Lipocalin-2

Introduction

Lipocalin 2 (LCN2) belongs to the lipocalin family. Members of this family transport small hydrophobic molecules such as lipids, steroid hormones and retinoids. The protein encoded by this gene is a neutrophil gelatinase-associated lipocalin and function in innate immunity by limiting bacterial growth as a result of sequestering iron-containing siderophores. The presence of this protein in blood and urine is an early biomarker of acute kidney injury. This protein is thought to be be involved in multiple cellular processes, including maintenance of skin homeostasis, and suppression of invasiveness and metastasis.

Entrez Gene ID

3934

UniProt ID

P80188

Alternative Names

24p3; MSFI; NGAL; p25

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme-Linked Immunospot (ELISpot)
Proteogenomics
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Isotype control

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

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