Analytical Data
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Gene name
Lcn3
- Application
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Alternative Names
Lipocalin-3 Vomeronasal secretory protein I Short name: VNSP I
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Species
Mouse
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q62471
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Expression Region
19-182aa
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Molecular Weight
34.7 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
LcN3, or lactoferrin C-terminal domain protein 3, is an intriguing biomolecule that has garnered attention in recent years due to its potential roles in various physiological processes and disease mechanisms. Research into LcN3 recombinant proteins has expanded as scientists seek to understand their functions, including antimicrobial activities and involvement in immune responses. Lactoferrins, which are glycoproteins predominantly found in secretory fluids, exhibit a range of bioactive properties, making their recombinant forms valuable for therapeutic applications. The LcN3 domain, in particular, has been implicated in modulating cellular interactions and regulating inflammation. Advances in recombinant DNA technology have facilitated the expression and purification of LcN3 proteins, allowing for detailed studies of their structural and functional characteristics. Investigating LcN3 recombinant proteins not only provides insights into the underlying biology of lactoferrins but also opens avenues for novel drug development and biotechnological applications. As research progresses, understanding the precise mechanisms by which LcN3 exerts its effects could lead to innovative strategies for managing infections and inflammatory diseases, highlighting the significance of this protein in both basic and applied sciences.
