Analytical Data
-
Gene name
LCN11
- Application
-
Species
Rat
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
B3EY86
-
Expression Region
Leu17~Leu177
-
Molecular Weight
22kDa
-
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
LCN11, or Lipocalin 11, is a member of the lipocalin superfamily, which is characterized by its ability to bind small hydrophobic molecules. Research on LCN11 has garnered attention due to its potential roles in various biological processes, including reproductive functions and metabolic regulation. Studies suggest that LCN11 may be involved in male fertility and the transport of retinoids, which are crucial for normal spermatogenesis and overall reproductive health. The characterization of recombinant LCN11 protein provides a valuable tool for elucidating its physiological functions and mechanisms of action. By producing this protein in vitro, researchers can investigate its binding affinities, structural properties, and interactions with other molecules. Understanding the role of LCN11 in health and disease could lead to the development of novel therapeutic strategies for treating infertility and metabolic disorders. Additionally, as lipocalins are implicated in various pathophysiological conditions, including obesity and cancer, LCN11 may represent a promising target for further research in these areas. Overall, the study of LCN11 recombinant protein is crucial for advancing knowledge in reproductive biology and expanding our understanding of lipocalin functions in human health.
