Analytical Data
-
Gene name
NPIP
- Application
-
Alternative Names
NPIP
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
A6NHP6
-
Expression Region
1-128 aa
-
AA Sequence
MVDGQPSLQQVLERVDEWMAKEGLLDPNVKSIFVTCGDWDLKVMLPGQCQYLGLPVADYFKQWINLKKAYSFAMGCWPKNGLLDMNKGLSLQHIGRPHSGIDDCKNIANIMKTLAYRGFIFKQTSKPF
-
Molecular Weight
40.9 kDa
-
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
NPIP (Nuclear Protein Interactor of Serine/Arginine-rich Splicing Factors) is a group of proteins that have garnered interest due to their significant roles in various cellular processes, including RNA splicing, transcription regulation, and the DNA damage response. Recent studies have highlighted the multifunctional nature of NPIPs, which are involved in the regulation of gene expression and might play critical roles in the development of diseases such as cancer. As the understanding of the molecular mechanisms underlying these processes expands, researchers are increasingly focusing on the recombinant production of NPIP proteins to elucidate their structure and function. Recombinant protein techniques enable the generation of large quantities of these proteins, facilitating in-depth biochemical and biophysical characterizations. Furthermore, this approach allows scientists to investigate NPIPs' interactions with other cellular molecules, paving the way for potential therapeutic applications. The exploration of NPIPs is particularly relevant in the context of cancer biology, where aberrant splicing and gene expression often contribute to tumorigenesis. By producing and studying NPIPs in a controlled setting, researchers aim to uncover new insights that could lead to targeted treatment strategies. Overall, the recombinant study of NPIP proteins is a crucial step toward understanding their intricate roles in cellular function and pathology, ultimately contributing to advancements in medical science and therapeutic development.











