protein

SRSF1 Protein, Human (His-SUMO)

HY-P700524

10 μg;50 μg;100 μg

80;200;335 USD

SRSF1 Protein, Human (His-SUMO)

proteins

E. coli

10 μg;50 μg;100 μg

80;200;335 USD

The SRSF1 protein plays a crucial role in splicing regulation, preventing exon skipping and ensuring splicing accuracy. It interacts with spliceosome components and forms a bridge between 5'- and 3'-splice site binding elements. SRSF1 Protein, Human (His-SUMO) is the recombinant human-derived SRSF1 protein, expressed by E. coli , with N-SUMO, N-6*His labeled tag. The total length of SRSF1 Protein, Human (His-SUMO) is 247 a.a.

Human

SRSF1 protein plays a crucial role in maintaining splicing fidelity by preventing exon skipping and regulating alternative splicing. Its interaction with spliceosomal components, facilitated by RS domains, establishes a bridge between the 5'- and 3'-splice site binding elements, U1 snRNP and U2AF. SRSF1 exhibits preferential binding to purine-rich RNA sequences, acting as a splicing enhancer in vitro through the ASF/SF2 splicing enhancer (ASE). While isoforms ASF-2 and ASF-3 function as splicing repressors, SRSF1 may also serve as an export adapter in mRNA nuclear export via the TAP/NXF1 pathway. Within the spliceosome C complex, it collaborates with other RNA-binding proteins, including DDX5, HNRNPH2, and splicing regulator ARVCF. SRSF1's extensive interactome involves proteins such as SAFB/SAFB1, PSIP1/LEDGF, RSRC1, ZRSR2/U2AF1-RS2, CCDC55, SRPK1, NXF1, CCNL1, CCNL2, CDK11B, and RRP1B, showcasing its multifaceted roles in RNA processing and cellular functions. Additionally, its interaction with TNPO3 facilitates nuclear import when phosphorylated in the RS domain, and it interacts with ILDR1 and ILDR2.

Alternative-splicing factor 1; ASF-1Splicing factor; arginine/serine-rich 1pre-mRNA-splicing factor SF2; P33 subunit

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris-HCL, 200 mM NaCl, 0.1%SKL, pH 8.0.

Room temperature in continental US; may vary elsewhere.