Analytical Data
-
Gene name
NASP
- Application
-
Species
Rat
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
Q66HD3
-
Expression Region
Thr3~Asp223
-
Molecular Weight
27kDa
-
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
NASP (Nuclear Autosomal Recessive Splicing Factor) is a crucial nuclear protein that plays a significant role in the regulation of RNA splicing and ribosome biogenesis. Its involvement in cellular processes such as cell proliferation, differentiation, and response to stress makes it an important focus of research. Abnormal expression of NASP has been implicated in various cancers and other diseases, suggesting that it may serve as a potential biomarker or therapeutic target. Studies have revealed that NASP is essential for the proper assembly and transport of histone proteins, which are vital for DNA packaging and gene regulation. Moreover, its interactions with other cellular proteins indicate its function in orchestrating nuclear activities during cell cycle progression. Given these crucial roles, recombinant NASP proteins have been developed for detailed biochemical and structural studies, aimed at understanding the molecular mechanisms governing splicing and cell function. This research could provide insights into the pathological mechanisms associated with NASP dysregulation, paving the way for innovative strategies in cancer treatment and regenerative medicine. Researchers are increasingly focusing on characterizing the structure-function relationships of NASP through advanced techniques such as X-ray crystallography and NMR spectroscopy, contributing to a deeper understanding of its role in cellular processes. As such, the study of recombinant NASP protein is not only pivotal for elucidating its biological functions but also holds promise for therapeutic advancements.
