SECIS Binding Protein 2 (SECISBP2) ELISA Kits

Mouse (Murine) SECIS Binding Protein 2 (SECISBP2) interaction partners

1. Selenocysteine insertion sequence binding protein 2 (SBP2)conditional knockout (iCKO) mice replicate the thyroid phenotype of SBP2 deficiency for investigating selenoprotein biology relevant to human disease.

2. The results demonstrate that Secisbp2 is not strictly required for Sec incorporation and has a distinct role in stabilizing mRNAs that can be separated from its effects on UGA-redefinition

3. Secisbp2 is essential for embryonic development and enhances selenoprotein expression.

4. SBP2/SECIS complex activates eEFSec by directing functional interactions between Domain IV and the ribosome to promote Sec-tRNA(Sec) binding and accommodation into the ribosomal A-site

5. Selenocysteine insertion sequence (SECIS)-binding protein 2 alters conformational dynamics of residues involved in tRNA accommodation in 80 S ribosomes.

Fruit Fly (Drosophila melanogaster) SECIS Binding Protein 2 (SECISBP2) interaction partners

1. Swapping only five amino acids between dSBP2 and human SBP2 in the K-rich domain conferred reversed SECIS-binding properties to the proteins, thus unveiling an important sequence for form 1 binding.

Human SECIS Binding Protein 2 (SECISBP2) interaction partners

1. SBP2 interacts directly with four proteins of the SMN complex and the methylosome core proteins.

2. SBP2 makes direct contacts with a discrete region of the human 28S rRNA.

3. The patient showed typical symptoms of SBP2 deficiency, and novel compound heterozygous mutations were identified in SBP2 (p.M515fsX563/p.Q79X).

4. Selenocysteine insertion sequence (SECIS)-binding protein 2 alters conformational dynamics of residues involved in tRNA accommodation in 80 S ribosomes.

5. Describe subjects with compound heterozygous defects in the SECISBP2 gene. These individuals have reduced synthesis of most of the 25 known human selenoproteins, resulting in a complex phenotype.

6. Results demonstrate that SECIS-binding protein 2 is required for protection against reactive oxygen species-induced cellular damage and cell survival.

7. In addition to identifying key amino acids for SECIS recognition by SBP2, our findings led to the proposal that some of the recognition principles governing the 15.5 kD-U4 snRNA interaction must be similar in the SBP2-SECIS RNA complex

8. Oxidative stress induces nuclear accumulation of SBP2 via oxidation of cysteine residues within a redox-sensitive cysteine-rich domain.

9. Data suggest that SBP2 is a major determinant in dictating the hierarchy of selenoprotein synthesis via differential selenoprotein mRNA translation and sensitivity to nonsense-mediated decay.

10. SECIS binding induces a conformational change in SBP2 that recruits eEFSec, which in concert with the Sec incorporation domain gains access to the ribosomal A site