DIM1 / TXNL4A Protein (His Tag)

Thioredoxin-like 4A Protein Datasheet

DIM1 / TXNL4A Protein Product Information

• Synonym: DIB1, DIM1, HsT161, TXNL4, U5-15kD
• Protein Construction: A DNA sequence encoding the human TXNL4A (P83876) (Met 1-Tyr 142) was expressed, with a polyhistidine tag at the N-terminus.
• Source: Human
• Expression Host: E.coli

DIM1 / TXNL4A Protein QC Testing

• Purity: > 94 % as determined by SDS-PAGE
• Endotoxin: Please contact us for more information.
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Met
• Molecular Mass: The recombinant human TXNL4A consists of 157 amino acids and has a calculated molecular mass of 18.6KDa. It migrates as an approximately 16 kDa band in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from sterile 50mM Tris,150mM NaCl; pH8.0.
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: DIM1 / TXNL4A protein

DIM1 / TXNL4A Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

DIM1 / TXNL4A Protein Description

DIM1, also known as TXNL4A, is a member of the Dim protein family. There are two members in the Dim protein family, DIM1and Dim2. They share a common thioredoxin-like fold. These two proteins were originally identified for their role in cell cycle progression and have been found to interact with Prp6, an essential component of the spliceosome, which forms the bridge of U4/U6.U5-tri-snRNP. In spite of their biological and structural similarities, DIM1 and Dim2 proteins differ in many aspects. DIM1 bears distinctive structural motifs responsible for its interaction with other spliceosome components. Dim2 forms homodimers and contains specific domains required for its interactions with partners. This originality suggests that although both proteins are involved in pre-mRNA splicing, they are likely to be involved in different biological pathways. DIM1 interacts with HNRPF, HNRPH2, NEDD9/HEF1 and PQBP1/NPW38. It plays an essential role in pre-mRNA splicing.

References

1. Zhang Y. et al., 2001, Gene. 257 (1): 33-43.
2. Zhang YZ. et al., 2003, Biochemistry. 42 (32): 9609-18.
3. Zhang YZ. et al., 2000, Physiol Genomics. 1 (3): 109-18.