ASF or called SF2, a member of the SR protein family, is an essential pre-mRNA splicing factor required for both single and alternative splicing (1-3). Phosphorylation on serine residues located within the SR domain directly regulates ASF/SF2 activity and compartmentalization of other SR splicing factors (4, 5). In addition to interacting with RNA and other splicing factors, such as U1-70K, U2AF and other SR proteins, ASF/SF2 also directly or indirectly interacts with HIV regulatory protein Rev, the C-terminal domain (CTD) of the largest subunit of RNA polymerase II, and numerous transcription factors, thereby suggesting a potential role of ASF/SF2 in coordinating of transcription and pre-mRNA splicing (6, 7).

Recombinant ASF/SF2 protein can be used for: 1) in vitro function studies including pre-mRNA splicing, cross linking and other RNA binding assays; 2) protein-protein interaction assay; and 3) cell growth and proliferation assays.

SC35, a member of the SR protein family, is an essential pre-mRNA splicing factor and can function as an essential splicing factor as well as an alternative splicing factor (1, 2). Phosphorylation of serine residues located within the SR domain directly regulates SC35 activity and compartmentalization of other SR splicing factors (3, 4). In addition to interacting with RNA and other splicing factors, SC35 has been shown to interact either directly or indirectly with the C-terminal domain (CTD) of the largest subunit of RNA polymerase II, thereby suggesting a potential role of SC35 in coordinating transcription and pre-mRNA splicing (5, 6).

The human SC35 wild type protein was expressed in a baculovirus system and purified by affinity and FPLC chromatography.

Recombinant SC35 protein can be used for: 1) in vitro function studies including pre-mRNA splicing, cross linking and other RNA binding assays; 2) protein-protein interaction assay; and 3) cell growth and proliferation assays.

The purified protein is greater than 95% homogeneous based on SDS-PAGE analysis.
1 unit equals 1 nanogram of purified protein. 1-5 units are sufficient for a gel mobility shift assay in a 20 µl reaction, 100 units are sufficient for a protein-protein interaction assay and 100-500 units are required for a splicing assay in a 20 μl reaction.

Concentration is variable in different lots.

Supplied in 1x buffer B: 20 mM HEPES-Na (pH 7.9), 20% Glycerol, 42 mM (NH4)2SO4, 0.5 mM DTT and 0.2 mM EDTA

References:
1. Ge, H., et al., (1990) Cell 62, 25-34; (1991) Cell 66, 373-382
2. Krainer, A.R., et al., (1990) Cell 62, 35-42; (1991) Cell 66, 383-394
3. Zahler, A.M., et al., (1992) Genes & Dev. 6, 837-847
4. Gui, J.F., et al., (1994) Proc. Natl. Acad. Sci. USA 91, 10824-10828
5. Colwill, K., et al., (1996) EMBO J. 15, 265-275
6. Tange, T.O., et al., (1996) J. Biol. Chem. 271, 10066-10072
7. Mortillaro, M.J., et al., (1997) Proc. Natl. Acad. Sci. USA 93, 8253-8257
8. Benz et al., (2005) Blood, Vol.105, No.5,2146-2153

DISCLAIMER

This products is recommended For RESEARCH USE ONLY and is Not qualified for Use in Diagnostic or Therapeutic Procedures.