Analytical Data
-
Gene name
LCN8
- Application
-
Alternative Names
LCN5; Epididymal-specific lipocalin-8
-
Species
Mouse
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
Q924P3
-
Expression Region
Leu27~Val176
-
Molecular Weight
21kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
LCN8, or lipocalin 8, is a member of the lipocalin family, which is known for binding small hydrophobic molecules and facilitating their transport within biological systems. This protein has garnered interest due to its potential roles in various physiological and pathological processes, including its involvement in mammalian reproduction and its potential implications in cancer biology. Studies have suggested that LCN8 may influence cell signaling and differentiation, making it a candidate for exploratory research in tumor biology and other diseases. The recombinant production of LCN8 allows for a deeper understanding of its structure-function relationships and biological activities, enabling researchers to investigate its mechanisms of action and interactions with other biomolecules. Furthermore, the use of recombinant protein techniques facilitates large-scale production and characterization, ensuring that researchers can perform in vitro and in vivo studies to elucidate the role of LCN8 in health and disease. As research progresses, LCN8 could emerge as a valuable biomarker or therapeutic target, underscoring the importance of comprehensive studies in elucidating its biological significance.
