Lipocalin-2/NGAL Protein, Human

Lipocalin-2/NGAL is an iron transporter that plays a crucial role in various cellular processes. It interacts with the siderophore 2,3-DHBA to transport iron into or out of cells depending on cellular needs. Lipocalin-2/NGAL Protein, Human is the recombinant human-derived Lipocalin-2/NGAL protein, expressed by E. coli , with tag free.

Lipocalin-2/NGAL, an iron-trafficking protein, plays a pivotal role in diverse cellular processes, including apoptosis, innate immunity, and renal development. Through its interaction with the siderophore 2,3-dihydroxybenzoic acid (2,3-DHBA), bearing structural resemblance to bacterial enterobactin, Lipocalin-2/NGAL serves as a versatile mediator for the transport of iron into or out of cells, contingent on specific cellular requirements. The iron-bound form (holo-24p3) undergoes internalization upon binding to the SLC22A17 (24p3R) receptor, leading to the liberation of iron and a subsequent rise in intracellular iron concentration. Conversely, the association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor initiates a cascade involving an intracellular siderophore, resulting in iron chelation and subsequent extracellular iron transfer, ultimately reducing intracellular iron levels. In the context of apoptosis induced by interleukin-3 (IL3) deprivation, the iron-loaded form augments intracellular iron concentration without triggering apoptosis, while the iron-free form diminishes intracellular iron levels, inducing the expression of the proapoptotic protein BCL2L11/BIM, thereby promoting apoptosis. Lipocalin-2/NGAL's involvement in innate immunity manifests as it restricts bacterial proliferation by sequestering iron bound to microbial siderophores, such as enterobactin. Furthermore, Lipocalin-2/NGAL exhibits the ability to bind siderophores from M.tuberculosis. Its structural arrangements include a monomeric state and a homodimer linked by disulfide bonds, as well as a heterodimeric form in association with MMP9.

Measured by its ability to bind Iron(III) dihydroxybenzoic acid [Fe(DHBA)3] in 30 min at 25°C. The binding of Fe(DHBA)3 results in the quenching of Trp fluorescence in 2μM NGAL. >1.5 μM of Fe(DHBA)3 can be bound.

Human

E. coli

Tag Free

P80188-1 (Q21-G198)

3934  [NCBI]

QDSTSDLIPAPPLSKVPLQQNFQDNQFQGKWYVVGLAGNAILREDKDPQKMYATIYELKEDKSYNVTSVLFRKKKCDYWIRTFVPGCQPGEFTLGNIKSYPGLTSYLVRVVSTNYNQHAMVFFKKVSQNREYFKITLYGRTKELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDG

Approximately 21 kDa

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  Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized from a 0.2 μm solution of PBS with 0.05 % Tween-20, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in sterile distilled water.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.