Analytical Data
-
Gene name
U4A/SNRPA
- Application
-
Alternative Names
(U1 snRNP A)(U1-A)(U1A)
-
Species
Mouse
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q62189
-
Expression Region
1-287aa
-
Molecular Weight
39.3 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
U4A/SNRPA is a key protein involved in the regulation of pre-mRNA splicing, a critical process in gene expression. Research into U4A/SNRPA has gained momentum due to its essential role in spliceosome formation, which is crucial for the accurate removal of introns from precursor mRNA and the subsequent ligation of exons. Splicing is fundamental for generating protein diversity and proper gene regulation, and any dysregulation in this process can lead to various diseases, including cancer and neurodegenerative disorders. Recent studies have focused on the structural and functional aspects of U4A/SNRPA, aiming to understand how it interacts with other spliceosomal components and contributes to the splicing machinery's overall dynamics. The investigation of U4A/SNRPA also holds potential for therapeutic applications, as targeting splicing mechanisms may provide innovative strategies to rectify splicing-related maladies. Overall, understanding the behavior of U4A/SNRPA and its role in the splicing process is vital for advancing knowledge in molecular biology and developing effective treatment approaches for related diseases.
