Analytical Data
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Gene name
LCN1/Lipocalin-1
- Application
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Alternative Names
(Tear lipocalin)(Tlc)(Tear prealbumin)(TP)(Von Ebner gland protein)(VEG protein)
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Species
Pig
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Source
E. coli
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P53715
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Expression Region
20-176aa
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Molecular Weight
24.3 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
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Protein Description
LCN1, also known as Lipocalin-1, is a member of the lipocalin family of proteins that play a pivotal role in various biological processes, including immune response, inflammation, and tissue remodeling. Initially discovered in the context of mammalian development, LCN1 has garnered significant attention due to its involvement in cancer progression, particularly in relation to tumor growth and metastasis. Elevated levels of LCN1 have been correlated with poor prognosis in various cancers, leading to investigations into its functional mechanisms and potential as a therapeutic target. The recombinant expression of LCN1 has become a focal point of research, as it allows for the detailed study of its structure-function relationships, as well as its interactions with other biomolecules. This research is essential for understanding how LCN1 influences tumor microenvironments and systemic pathways. The production of recombinant LCN1 not only facilitates biochemical assays but also opens avenues for developing novel diagnostic and therapeutic strategies aimed at modulating LCN1 activity. Furthermore, studying the post-translational modifications and regulatory mechanisms governing LCN1 expression can provide deeper insights into its role in health and disease, potentially leading to improved treatment options for cancer patients.











