Analytical Data
-
Gene name
SNRPC
- Application
-
Alternative Names
SNRPC;U1 small nuclear ribonucleoProtein C
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P09234
-
Expression Region
1-159aa
-
AA Sequence
MPKFYCDYCDTYLTHDSPSVRKTHCSGRKHKENVKDYYQKWMEEQAQSLI DKTTAAFQQGKIPPTPFSAPPPAGAMIPPPPSLPGPPRPGMMPAPHMGGP PMMPMMGPPPPGMMPVGPAPGMRPPMGGHMPMMPGPPMMRPPARPMMVPT RPGMTRPDR
-
Molecular Weight
44 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
SNRPC, or Small Nuclear Ribonucleoprotein Polypeptide C, is a crucial component of the spliceosomal machinery in eukaryotic cells, playing a vital role in the splicing of pre-mRNA. The study of SNRPC is significant due to its implications in gene regulation, RNA processing, and various cellular functions. Alterations in SNRPC expression or function can lead to a range of diseases, including cancer and neurodegenerative disorders, highlighting the need for a deeper understanding of its structure and mechanisms. Research has shown that SNRPC is involved in the assembly of spliceosomal complexes and interacts with various RNA and protein factors, which are essential for accurate splicing. Moreover, recent studies have suggested that SNRPC may also have roles in other cellular processes beyond splicing, such as transcription regulation and maintaining cellular homeostasis. This expanding knowledge of SNRPC's multifaceted roles underscores its importance as a target for therapeutic intervention and as a subject of study in the fields of molecular biology and genetics. Understanding the molecular dynamics and interactions of SNRPC can potentially lead to new strategies for treating diseases associated with spliceosomal dysfunctions. Thus, ongoing research is focused on elucidating the structural characteristics of SNRPC and its interactions in the context of the spliceosome and beyond, aiming to contribute to the broader field of RNA biology and its implications for human health.
