Analytical Data
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Gene name
LCN2
- Application
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Alternative Names
LCN2；HNL；NGAL；Neutrophil gelatinase-associated lipocalin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P80188
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Expression Region
21-198aa
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AA Sequence
QDSTSDLIPA PPLSKVPLQQ NFQDNQFQGK WYVVGLAGNA ILREDKDPQK MYATIYELKE DKSYNVTSVL FRKKKCDYWI RTFVPGCQPG EFTLGNIKSY PGLTSYLVRV VSTNYNQHAM VFFKKVSQNR EYFKITLYGR TKELTSELKE NFIRFSKSLG LPENHIVFPV PIDQCIDG
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Molecular Weight
20.5 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Lipocalin 2 (LCN2), also known as 24p3 or NGAL (neutrophil gelatinase-associated lipocalin), is a small extracellular protein that plays crucial roles in various biological processes, including iron homeostasis, immune response, and inflammation. It is primarily produced by neutrophils and various epithelial cells in response to inflammatory stimuli. The interest in LCN2 has surged due to its implications in several disease states, including cancer, renal injury, and infections. Its ability to bind iron and transport it in the extracellular environment makes it a key player in regulating the iron levels within tissues, thereby influencing microbial growth and the host's immune response. Furthermore, LCN2 is regarded as a potential biomarker for acute kidney injury and is being studied for its diagnostic and therapeutic potentials. The production of recombinant LCN2 proteins through genetic engineering techniques has facilitated the detailed exploration of its biological functions and interactions. By studying the structure-function relationship of LCN2, researchers aim to uncover its mechanistic roles in pathophysiological conditions and to develop novel therapeutic strategies that leverage its properties. Overall, the recombinant expression and characterization of LCN2 hold promise not only for advancing our understanding of its biological significance but also for its potential applications in clinical diagnostics and therapeutics.
