Analytical Data
-
Gene name
NOLC1
- Application
-
Alternative Names
P130; NOPP130; NOPP140; NS5ATP13; Nucleolar Phosphoprotein p130; 140 kDa nucleolar phosphoprotein; Hepatitis C virus NS5A-transactivated protein 13
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q14978
-
Expression Region
Thr384~Lys587
-
Molecular Weight
34kDa
-
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
NOLC1, or nucleolar and coiled-body phosphoprotein 1, is a key protein involved in various cellular processes, including ribosome biogenesis and nucleolar function. Its role in the assembly and function of the nucleolus, a crucial organelle for ribosomal RNA synthesis and processing, highlights its importance in cellular homeostasis and stress responses. Research has shown that NOLC1 is implicated in several diseases, including cancer, where its expression levels often correlate with tumor progression and patient prognosis. Given the protein's essential functions and its potential as a biomarker or therapeutic target, recombinant NOLC1 has gained attention in the scientific community. Studies focusing on the characterization of recombinant NOLC1 allow for a deeper understanding of its structural and functional properties. This research is crucial for elucidating the molecular mechanisms underlying its role in normal physiology and disease states. Furthermore, exploring the interactions of NOLC1 with other nucleolar components may provide insights into the regulatory networks governing ribosome biogenesis. As a result, recombinant forms of NOLC1 can serve as valuable tools for both basic research and potential clinical applications, paving the way for novel strategies in cancer therapeutics and diagnostics.











