Recombinant Human TXNL4A protein
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Recombinant Human TXNL4A protein is a Human Full Length protein, in the 1 to 142 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
DIM1, TXNL4, TXNL4A, Thioredoxin-like protein 4A, DIM1 protein homolog, Spliceosomal U5 snRNP-specific 15 kDa protein, Thioredoxin-like U5 snRNP protein U5-15kD
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human TXNL4A protein (AB126672)
15% SDS-PAGE analysis of 3µg ab126672.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
TXNL4A functions as part of the survival of motor neuron (SMN) complex which is responsible for the assembly of small nuclear ribonucleoproteins (snRNPs). SnRNPs are fundamental components of the spliceosome the molecular machine that performs pre-mRNA splicing. TXNL4A contributes to the synthesis of spliceosomal snRNPs influencing gene expression regulations. It interacts with several specific proteins within the SMN complex to ensure proper snRNP assembly and maturation.
Pathways
TXNL4A plays an important role in the spliceosome pathway and the mRNA processing pathway. Its interactions in the spliceosome pathway are important for the regulation of alternative splicing which greatly expands protein diversity. TXNL4A interacts with other proteins such as SMN1 and Gemin2 within this pathway coordinating the assembly of snRNPs. In the mRNA processing pathway the accurate execution of pre-mRNA splicing affects downstream physiological processes.
Specifications
Form
Liquid
Additional notes
ab126672 is purified using conventional chromatography techniques.
General info
Function
Plays a role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes that are involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex).
Sequence similarities
Belongs to the DIM1 family.
Post-translational modifications
The disulfide bond seen in structures determined by X-ray crystallography (PubMed:10610776) and NMR (PubMed:12911302) is not essential for protein folding and function (PubMed:12911302, PubMed:17467737).
Subcellular localisation
Nucleus
Target data
Product promise
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