Analytical Data
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Gene name
LCN4
- Application
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Alternative Names
VNSP2; Vomeronasal secretory protein II
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Species
Mouse
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q62472
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Expression Region
Tyr20~Ser178
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Molecular Weight
48kDa
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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
The LCN4 (lipocalin 4) protein, also known as the fetal antigen-1, is a member of the lipocalin family, which is characterized by a common structural motif of an 8-stranded β-barrel. LCN4 has garnered attention due to its significant roles in various physiological and pathological processes, including adipogenesis, cellular signaling, and potential involvement in reproductive functions. Research indicates that LCN4 may act as a biomarker for certain types of cancer, particularly in breast and prostate tissues, and it is implicated in metabolic disorders and obesity-related conditions. The recombination and expression of LCN4 as a fusion protein have opened new avenues for studying its functional roles at the molecular level, allowing researchers to investigate its interactions with other proteins and its effects on cellular behaviors. Furthermore, understanding the structure-function relationship of LCN4 through recombinant technology can aid in developing therapeutic strategies that target its pathways, thus holding promise for clinical applications in oncology and metabolic disease management. As research in this area progresses, LCN4 may emerge as a vital target for drug development and diagnostic applications, underscoring the importance of detailed studies on this intriguing lipocalin.
