protein

LCN2 Human, Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Human Recombinant Protein, Pichia

PROTP80188

5 ug, 20 ug, 1 mg

LCN2 Human, Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Human Recombinant Protein, Pichia

https://www.bosterbio.comlcn2-human-neutrophil-gelatinase-associated-lipocalin-lipocalin-2-human-recombinant-protein-pichia-protp80188-boster.html

LCN2

5 ug, 20 ug, 1 mg

Mouse

Cell Culture

Introduction: Recombinant Human Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core. They thereby serve as transporters of substances like retinal, biliverdins prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.

Neutrophil Gelatinase Associated Lipocalin Human Recombinant is expressed in Pichia pastoris having a molecular weight of approximately 21kDa. The LCN2 is purified by proprietary chromatographic techniques.

Pichia pastoris.

Sterile Filtered White lyophilized (freeze-dried) powder.

LCN2 was lyophilized from 0.02M NH4

Greater than 96% as determined by SDS-PAGE.

Lyophilized LCN2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCN2 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

P80188

Neutrophil gelatinase-associated lipocalin

Neutrophil gelatinase-associated lipocalin;NGAL;25 kDa alpha-2-microglobulin-related subunit of MMP-9;Lipocalin-2;Oncogene 24p3;Siderocalin LCN2;p25;LCN2;HNL, NGAL;

Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development. Binds iron through association with 2,5-dihydroxybenzoic acid (2,5- 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. Involved in innate immunity, possibly by sequestrating iron, leading to limit bacterial growth.

Secreted

Expressed in bone marrow and in tissues that are prone to exposure to microorganism. High expression is found in bone marrow as well as in uterus, prostate, salivary gland, stomach, appendix, colon, trachea and lung. Not found in the small intestine or peripheral blood leukocytes.