Human Lipocalin 2, LCN2 ELISA Kit
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Lipocalin-2 (also known as Neutrophil gelatinase-associated lipocalin or NGAL) is an iron binding and iron trafficking protein. Lipocalin-2 is involved in multiple cellular processes including apoptosis, innate immunity and renal development. Mice deficient in Lipocalin-2 appear normal but have increased susceptibility to bacterial infection. The bacteriostatic function may be related to Lipocalin-2 limiting bacterial iron supply. Human Lipocalin-2 has 62% protein sequence identity to mouse Lipocalin-2.
Fully tested in-house by ABMIUM, or supported by an advanced validation report from a partner reviewed by ABMIUM. Highest confidence. Non-conformities fully supported under the ABMIUM Product Promise.
Quality verified. Independent collaborator or expected-performance data available. Product meets ABMIUM quality standards.
Expected to work based on structural and biochemical data. Not yet directly tested by ABMIUM or a collaborator. No non-conformity support for this combination.
Not recommended for this application or species/sample combination. This may indicate either evidence of unsuitability or that the combination has not been tested and therefore cannot currently be recommended.
Evidence status by application and model.
| Evidence | Serum | Plasma | Urine | Ascites | Cerebrospinal fluid | Tissue | Cell culture supernatants | Tissue homogenates |
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| Compatibility |
This product is manufactured by BT LAB and sold through ABMIUM without relabelling.
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Yes. Send your target, sample, application and experimental conditions through ABMIUM MATCH or technical support.
Unless the listing expressly states otherwise, ABMIUM products are supplied for research use only and are not for diagnostic or therapeutic use.
LCN2 identifies lipocalin 2 in Homo sapiens (Human). This target record connects NCBI Gene 3934, UniProtKB P80188 and related ABMIUM catalogue products.
Biological function: LCN2 (NGAL) is an iron-trafficking lipocalin involved in innate immunity and other cellular processes. It binds iron-associated siderophores and can alter cellular iron availability depending on context.
