SF1 Antibodies

Structure of SF1

Splicing factor 1 encoded by the SF1 gene is a nucleoprotein with a molecular weight of approximately 34-36 kDa, and its precise molecular weight varies slightly among different species.

The SF1 protein is composed of approximately 300 amino acids, and its three-dimensional structure contains two key functional domains: the KH (K homology) domain at the N-terminal is responsible for recognizing RNA sequences, while the zinc finger structure at the C-terminal participates in protein-protein interactions. This protein forms a stable RNA binding interface through the α -helix and β -folding in its secondary structure, in which the conserved GGNG motif directly binds to the pre-mRNA branch site. SF1 plays a scaffold role in the early stage of spliceosome assembly, and its conformational changes can regulate splicing efficiency. However, mutations in certain key amino acids (such as Arg240 and Lys303) can lead to splicing errors and are associated with various genetic diseases.

Fig. 1 Cartoon of SF-1 showing key functional domains and the position of the two SF-1 variants associated with this phenotype.¹

Key structural properties of SF1:

• KH domain with zinc finger motif
• Conserved RNA binding interface
• Dynamic conformation regulation
• Key functional sites

Functions of SF1

The core function of the SF1 gene is to regulate pre-mRNA splicing and participate in the regulation of multiple gene expression processes simultaneously.

The binding curve of the SF1 and U2AF complex is synergistic (nonlinear), reflecting its characteristic of dynamically regulating splicing efficiency through conformational changes. The latest research in "Nature Structural & Molecular Biology" reveals that the phosphorylation state of SF1 can change its RNA binding affinity and achieve differential splicing regulation during the cell cycle.

Applications of SF1 and SF1 Antibody in Literature

1. Wang, Xinyue, et al. "A novel rabbit anti-myoglobin monoclonal antibody's potential application in rhabdomyolysis associated acute kidney injury." International Journal of Molecular Sciences 24.9 (2023): 7822. https://doi.org/10.1007/s00401-024-02686-1

This study analyzed 270 cases of growth hormone-cell pituitary neuroendocrine tumors (PitNETs) and found that 74% of dense granular type (DGST) simultaneously expressed PIT1/SF1, and there were significant differences in clinicopathological and molecular characteristics compared with simple PIT1-positive DGST. The research suggests that such tumors co-expressing PIT1/SF1 should be classified separately as "growth gonadotropin cells PitNET", and it is recommended to revise the WHO classification standard.

2. Li, Xue, et al. "CXCR4-SF1 bifunctional adipose-derived stem cells benefit for the treatment of Leydig cell dysfunction-related diseases." Journal of Cellular and Molecular Medicine 24.8 (2020): 4633-4645. https://doi.org/10.1111/jcmm.15128

In this study, bifunctional adipose-derived stem cells (CXCR4-SF1-ADscs) expressing both CXCR4 and SF1 were constructed, which can be directed to migrate to the damaged testicles and differentiate into Leydig-like cells to repair BPA-induced Leydig cell dysfunction. Research has found that SF1 promotes testosterone synthesis by regulating the BSPRY gene, providing a new strategy for the treatment of Leydig cell dysfunction.

3. Godavarthi, Jyotsna D., et al. "Deficiency of Splicing Factor 1 (SF1) reduces intestinal polyp incidence in ApcMin/+ Mice." Biology 9.11 (2020): 398. https://doi.org/10.3390/biology9110398

Research has found that a reduction in the level of splicing factor SF1 can inhibit the formation of intestinal polyps in mice. In ApcMin/+ mutant mice, SF1 heterozygous deletion (Sf1+/−) reduced the number of polyps by 25-30%, especially in females and small polyps (≤2mm), suggesting that targeted reduction of SF1 may become a new strategy for preventing intestinal tumors.

4. Crisci, Angela, et al. "Mammalian splicing factor SF1 interacts with SURP domains of U2 snRNP-associated proteins." Nucleic acids research 43.21 (2015): 10456-10473. https://doi.org/10.1093/nar/gkv952

Studies have found that the splicing factor SF1 binds to the U2 snRNP protein through its conserved SURP interaction domain, recruiting U2 snRNP in the early formation of the spliceosome E complex. Experiments have confirmed that SF1 can pre-protrusion branch point sequences, promoting U2 snRNA pairing, and U2AF65 subsequently stabilizes this binding. The absence of SF1 reduces the formation of the A complex, suggesting its crucial role in the regulation of alternative splicing.

5. Barnea, Efrat, and Yehudit Bergman. "Synergy of SF1 and RAR in Activation of Oct-3/4Promoter." Journal of Biological Chemistry 275.9 (2000): 6608-6619. https://doi.org/10.1074/jbc.275.9.6608

Studies have found that SF1 is co-expressed with the embryonic transcription factor Oct-3/4 in P19 embryonic cancer cells and is simultaneously downregulated during retinoic acid-induced differentiation. SF1 recognizes two sites on the Oct-3/4 promoter through its DNA-binding domain (SF1(a) is located within RAREoct), and forms a novel complex with the retinoic acid receptor to synergistically activate the Oct-3/4 promoter, revealing for the first time the mechanism by which SF1 regulates embryonic specific genes.

Creative Biolabs: SF1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality SF1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom SF1 Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our SF1 antibodies, custom preparations, or technical support, contact us at email.