SRSF1 Human, Sf9
Sf9, Baculovirus cells.
SRSF1, ASF, SF2, SF2p33, SFRS1, Splicing Factor, Arginine/Serine-Rich, 30-KD, A, Alternate Splicing Factor, SRp30a, ASF-1, Serine And Arginine Rich Splicing Factor 1, Pre-MRNA-Splicing Factor SF2, P33 Subunit, Splicing Factor, Arginine/Serine-Rich 1, Serine/Arginine-Rich Splicing Factor 1, Alternative-Splicing Factor 1, SR Splicing Factor 1, Splicing Factor 2.
Greater than 95.0% as determined by SDS-PAGE.
Description
SRSF1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 254 amino acids (1-248) and having a molecular mass of 28.5kDa. SRSF1 is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
Serine/arginine-rich splicing factor 1 (SFRS1), a member of the arginine/serine-rich splicing factor protein family, plays a crucial role in both constitutive and alternative pre-mRNA splicing. This protein binds to pre-mRNA transcripts and components of the spliceosome, influencing splicing by either initiating or inhibiting it based on the location of its binding site on the pre-mRNA. The splicing activation function of SFRS1 is regulated through phosphorylation and interactions with other proteins associated with splicing factors.
Recombinant human SRSF1, expressed in Sf9 insect cells using a baculovirus system, is a single, glycosylated polypeptide chain. It comprises 254 amino acids (residues 1-248) and has a molecular weight of 28.5 kDa. A 6-amino acid His-tag is fused to the C-terminus of SRSF1 to facilitate purification, which is achieved using proprietary chromatographic techniques.
The SRSF1 protein solution is provided at a concentration of 0.25 mg/ml and is formulated in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 100 mM KCl, 1 mM DTT, 0.2 mM EDTA, and 40% glycerol.
The purity of the SRSF1 protein is determined to be greater than 95.0% as assessed by SDS-PAGE analysis.
SRSF1, ASF, SF2, SF2p33, SFRS1, Splicing Factor, Arginine/Serine-Rich, 30-KD, A, Alternate Splicing Factor, SRp30a, ASF-1, Serine And Arginine Rich Splicing Factor 1, Pre-MRNA-Splicing Factor SF2, P33 Subunit, Splicing Factor, Arginine/Serine-Rich 1, Serine/Arginine-Rich Splicing Factor 1, Alternative-Splicing Factor 1, SR Splicing Factor 1, Splicing Factor 2.
Sf9, Baculovirus cells.
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR HSRSRSRTHH HHHH.
Product Science Overview
SRSF1 is a member of the serine/arginine-rich splicing factor (SRSF) family, characterized by the presence of serine/arginine-rich (RS) domains. These domains are essential for the protein’s function in splicing regulation. The protein is approximately 33 kDa in size and plays a vital role in both constitutive and alternative splicing of pre-mRNA .
SRSF1 influences splice site selection in a concentration-dependent manner, which means that its levels can determine the outcome of splicing events. It is involved in the recognition of splice sites and the assembly of the spliceosome, a complex responsible for the removal of introns from pre-mRNA . Additionally, SRSF1 mediates post-splicing activities such as mRNA nuclear export and translation .
SRSF1 is essential for all splicing reactions to occur and is involved in various biological processes, including:
High expression of SRSF1 has been observed to significantly influence cancer progression, particularly in osteosarcoma (OS). Studies have shown that SRSF1 expression is consistently upregulated in OS samples and cell lines. Overexpression of SRSF1 leads to enhanced cell proliferation, migration, and invasion, while its knockdown results in reduced growth and increased apoptosis . These findings suggest that SRSF1 could be a potential therapeutic target in cancer treatment.
Recombinant SRSF1 (Human, Sf9) refers to the human SRSF1 protein produced using the Sf9 insect cell expression system. This system is commonly used for the production of recombinant proteins due to its ability to perform post-translational modifications similar to those in mammalian cells. The recombinant protein is used in various research applications to study the function and regulation of SRSF1 in splicing and other cellular processes.
