Analytical Data
-
Gene name
U2AF1L4
- Application
-
Alternative Names
U2AF1L4；U2AF1-RS3；U2AF1L3；Splicing factor U2AF 26 kDa subunit
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8WU68
-
Expression Region
1-202aa
-
AA Sequence
MAEYLASIFGTEKDKVNCSFYFKIGVCRHGDRCSRLHNKPTFSQEVFTELQEKYGEIEEMNVCDNLGDHLVGNVYVKFRREEDGERAVAELSNRWFNGQAVHGNVPEVASATSCICGPFPRTSRGSSMGGDPGAGHPRGSILATIPERGTIGVPLITGMAASEALAPLPFTPNRDRCSWQDLSSKPPSLSCPILPRLPGSIM
-
Molecular Weight
49.0 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
U2AF1L4 is a member of the U2AF (U2 small nuclear RNA auxiliary factor) protein family, which plays a crucial role in pre-mRNA splicing. This protein is essential for the recognition of the 3' splice site, thereby influencing gene expression and RNA processing. Research into U2AF1L4 has gained momentum due to its potential implications in various diseases, particularly cancer, where splicing alterations can contribute to tumorigenesis and disease progression. Furthermore, mutations and dysregulation of splicing factors like U2AF1 have been implicated in hematological malignancies and solid tumors, underscoring the importance of understanding U2AF1L4's function and interaction with other spliceosomal components. Recent studies have focused on elucidating the structural biology of U2AF1L4, its binding dynamics, and how it interacts with RNA substrates, which could pave the way for novel therapeutic strategies targeting splicing processes. As the understanding of the link between splicing and disease deepens, U2AF1L4 emerges as a key player in the regulatory networks of gene expression, making it a significant focus for ongoing and future research in molecular biology and cancer therapeutics.
