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
LCN2 (Lipocalin-2) is a multifaceted protein involved in various physiological and pathological processes, including immune response, neuroprotection, and cancer progression. It is part of the lipocalin family, characterized by its ability to bind small hydrophobic molecules, such as fatty acids and hormones, which suggests a role in lipid transport and metabolism. Elevated levels of LCN2 have been associated with numerous conditions, including obesity, diabetes, and inflammatory diseases, indicating its potential as a biomarker for these disorders. In cancer research, LCN2 has been implicated in tumor progression and metastasis, often linked to promoting an inflammatory tumor microenvironment. Given its significant roles in these processes, the study of recombinant LCN2 protein has gained traction to elucidate its function further and explore its therapeutic potential. By employing recombinant DNA technology, researchers can produce LCN2 in substantial quantities, facilitating in vitro and in vivo studies. This allows for a better understanding of its interactions with receptors, downstream signaling pathways, and its role in various cellular contexts. Moreover, investigating LCN2's structure-function relationship could reveal novel mechanisms of action, paving the way for the development of targeted therapies in diseases where LCN2 is dysregulated. Overall, the study of LCN2 not only deepens our knowledge of its biological functions but also opens avenues for novel therapeutic interventions in metabolic and oncological diseases.
