Recombinant Human Serine/Arginine-Rich Splicing Factor 1 (SRSF1) Protein (His-SUMO)

Name: Recombinant Human Serine/Arginine-Rich Splicing Factor 1 (SRSF1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04476P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Serine/Arginine-Rich Splicing Factor 1 (SRSF1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q07955
Target Symbol	SRSF1
Synonyms	Alternative splicing factor 1; Alternative-splicing factor 1; arginine/serine-rich 1; ASF 1; ASF; ASF-1; ASF1; FLJ53078; MGC5228; P33 subunit; Pre mRNA splicing factor SF2 P33 subunit; pre-mRNA-splicing factor SF2; Serine/arginine-rich splicing factor 1; SF2; SF2P33; SFRS1; Splicing factor 2 alternate splicing factor; Splicing factor 2; Splicing factor; Splicing factor arginine/serine rich 1; SR Splicing factor 1; SRp30a; srsf1; SRSF1_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	SGGGVIRGPAGNNDCRIYVGNLPPDIRTKDIEDVFYKYGAIRDIDLKNRRGGPPFAFVEFEDPRDAEDAVYGRDGYDYDGYRLRVEFPRSGRGTGRGGGGGGGGGAPRGRYGPPSRRSENRVVVSGLPPSGSWQDLKDHMREAGDVCYADVYRDGTGVVEFVRKEDMTYAVRKLDNTKFRSHEGETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSRT
Expression Range	2-248aa
Protein Length	Full Length of Mature Protein
Mol. Weight	43.6kDa
Research Area	Transcription
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing. Isoform ASF-2 and isoform ASF-3 act as splicing repressors. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway.
Subcellular Location	Cytoplasm. Nucleus speckle.
Protein Families	Splicing factor SR family
Database References	HGNC: 10780 OMIM: 600812 KEGG: hsa:6426 STRING: 9606.ENSP00000258962 UniGene: PMID: 28799539 repeat RNA-sequestration of SRSF1 triggers the NXF1-dependent nuclear export of C9ORF72 transcripts retaining expanded hexanucleotide repeats PMID: 28677678 A -44 G to A "hot zone" putative functional noncoding variant of SRSF1 was found in an AML patient. It alters the binding activities of E2F6, ELF1, and ELK4, ELK4. PMID: 29764005 We now show that the ability of SRPK1 to mobilize SRSF1 from speckles to the nucleoplasm is dependent on active CLK1. Diffusion from speckles is promoted by the formation of an SRPK1-CLK1 complex that facilitates dissociation of SRSF1 from CLK1 and enhances the phosphorylation of several serine-proline dipeptides in this SR protein PMID: 29335301 Authors showed that Mir505-3p was capable of inhibiting tumor proliferation driven by SRSF1 in two neural tumor cell lines, Neuro-2a (N2a) and U251, exclusively in serum-reduced condition. Authors observed that the protein level of SRSF1 was gradually promoted by increasing concentration of serum. PMID: 29120871 The present study suggested that the tumor suppressor miR30c may be involved in prostate cancer tumorigenesis, possibly via targeting ASF/SF2. PMID: 28677791 It has been proposed that SF2/ASF has a protective role against JC virus reactivation in multiple sclerosis patients. PMID: 27812788 Immune suppression of JC virus gene expression is mediated by SRSF1. PMID: 26951564 ASF/SF2 is identified as a splicing regulator of cyclin T1, which contributes to the control of the subsequent transcription events. PMID: 28422315 Findings suggest MALAT1 increases AKAP-9 expression by promoting SRPK1-catalyzed SRSF1 phosphorylation in CRC cells. These results reveal a novel molecular mechanism by which MALAT1 regulates AKAP-9 expression in CRC cells. PMID: 26887056 high level of SF2, as a novel oncoprotein in RCC, was significantly associated with poor survival in a large cohort of RCC specimens. Taken together, our study presents a road map for the prediction and validation of miR-766-3p/SF2 axis and thus imparts a therapeutic way for further RCC progression. PMID: 28657135 We present a joint atomistic molecular dynamics (MD) and experimental study of two RRM-containing proteins bound with their single-stranded target RNAs, namely the Fox-1 and SRSF1 complexes.The simulations predict unanticipated specific participation of Arg142 at the protein-RNA interface of the SRFS1 complex, which is subsequently confirmed by NMR and ITC measurements PMID: 27193998 Using NMR spectroscopy with two separately expressed domains of SRSF1, we showed that several residues in the RNA-binding motif 2 interact with the N-terminal region of the RS domain (RS1). PMID: 27091468 Especially, in SRSF1 morphants, bone cartilage formation was reduced in the brain and Nkx-2.5 expression was dramatically reduced in the heart of SRSF1 morphants. In addition, a dramatic reduction in functional chordin RNA in SRSF1 morphants was observed suggesting that chordin is one of the targets of SRSF1. Thus, we concluded that SRSF1 is an essential factor for pattern formation including heart, cartilage and germ lay PMID: 27396620 results strongly support SRSF1 as a prognostic biomarker in SCLC and provide a rationale for personalized therapy in SCLC PMID: 27093186 NSrp70 acts as a new molecular counterpart for alternative splicing of target RNA, counteracting SRSF1 and SRSF2 splicing activity. PMID: 26797131 we have identified for the first time a potential mechanism that involves the essential splicing factor ASF/SF2 through which morphine regulates splicing specificity of the MOR encoding gene, OPRM1. PMID: 26553431 Global splicing analysis with RNA-seq revealed that exons carrying the hnRNP H-binding GGGGG motif are predisposed to be skipped compared to those carrying the SRSF1-binding GGAGG motif in both human and mouse brains. PMID: 26282582 We present experimental evidence that splicing factor SRSF1, SRSF2, U2AF35, U2AF65 and KHSRP expression levels in gastrointestinal tract (colon, gastric and pancreatic) tumors differ compare to healthy tissues and in cell lines PMID: 26406946 These findings have revealed a molecular interplay between cellular SRSF1 and viral T-antigen in controlling JC virus gene expression. PMID: 26596376 These include alternative splicing of SRSF1 itself. PMID: 26273603 SF2 contributes to the elevated levels of ERK activation in hepatocellular carcinoma cells through modulating key component(s) downstream of growth factor receptors and upstream of ERK. PMID: 26018840 These results suggest that MALAT1 may function as a promoter of gastric cancer cell proliferation partly by regulating SF2/ASF. PMID: 24857172 SRSF1 regulates CD3zeta expression in human T cells and may contribute to the T cell defect in systemic lupus erythematosus. PMID: 26134847 serine/arginine-rich splicing factor 1 (SRSF1) could specifically interact with RIG-I to facilitate RIG-I mediated production of type-I IFN that is triggered by cytosolic DNA. PMID: 25658361 Using RNA-sequencing and 3-D cell cultures that mimic breast cancer, the authors identified SRSF1-regulated alternative splicing targets that are candidates for mediating SRSF1's oncogenic functions in mammary cells. PMID: 26431027 The accumulated knowledge about SRSF1 provides critical insight into the integral role it plays in maintaining cellular homeostasis and suggests new targets for anticancer therapy. PMID: 24807918 Data suggest that proline phosphorylation by CLK1/CDC-like kinase 1 (but not by SRPK1/serine/arginine-rich splicing factor kinase 1) regulates conformation and alternative splicing function of SFRS1 (serine/arginine-rich splicing factor 1). PMID: 25529026 SRSF1 is a critical regulator that controls both RNA splicing and stability in the nucleus and functions in a Malat1-dependent manner. PMID: 24468535 upon T cell activation, SRSF1 becomes limiting, and its function in CD6 exon 5 splicing is countered by an increase in CD6 transcription, dependent on chromatin acetylation. PMID: 24890719 Data indicate that armadillo repeat protein ARVCF interacts with the splicing factors the splicing factor SRSF1 (SF2/ASF), the RNA helicase p68 (DDX5), and the heterogeneous nuclear ribonucleoprotein hnRNP H2. PMID: 24644279 In the broader context of cancer pathology, the results suggest that SRSF1 might play a central role not only in the tumor cells, but also in the surrounding stroma. PMID: 23966470 results demonstrate a novel mechanism of regulation of the splicing factor SRSF1 in human T cells and a potential molecular mechanism that controls its expression in SLE. PMID: 24368769 Identification of new splicing events regulated by the oncogenic splicing factor SRSF1 in lung cancer using novel analytical tool. PMID: 24371231 Specific induction of AS2 due to Alternative splicing is associated with epithelial ovarian cancer. PMID: 23748175 Overexpression of SRSF1 and SRSF9 promote beta-catenin accumulation via the recruitment of beta-catenin mRNA and by enhancing its translation in an mTOR-dependent manner. PMID: 23592547 The data establish a new view of SRSF1 protein regulation in which SRPK1 and CLK1 partition activities based on Ser-Pro versus Arg-Ser placement rather than on N- and C-terminal preferences along the RS domain. PMID: 23707382 our results indicate that ASF/SF2 binds to a purine-rich region distant from both the previously published initiation site of HDV mRNA transcription and binding site of RNAP II, and suggest that this protein is not involved in HDV replication PMID: 23349975 a new mechanism of posttranscriptional regulation of DIO1 and show deregulation of DIO1 expression in pituitary adenoma, possibly resulting from disturbed expression of SF2/ASF. PMID: 23462647 High expression of ASF is associated with chronic myeloid leukemia. PMID: 23228155 Results indicate that SF2/ASF regulates IL-2 production and that decreased SF2/ASF expression in systemic lupus erythematosus (SLE) T cells contributes to deficient IL-2 production. PMID: 23319613 Results indicate that SRSF1 serves as an anti-apoptotic factor and potentially contributes to leukemogenesis in pediatric ALL patients by cooperating with PRMT1. PMID: 22839530 Data indicate that depletion of SRSF1 in human cells compromises the association of splicing factors to nuclear speckles and influences the levels and activity of other SR proteins. PMID: 22855529 SRSF1 is a direct target of the transcription factor oncoprotein MYC. PMID: 22545246 Overexpression of SRSF1 rescues apoptosis of MCF-7 cells induced by Pnn depletion. PMID: 22454513 In three-dimensional (3D) culture, SRSF1-overexpressing MCF-10A cells formed larger acini than control cells, reflecting increased proliferation and delayed apoptosis during acinar morphogenesis. PMID: 22245967 ASF/SF2 translocates to the cytosol and regulates the alternative splicing of endoglin during senescence of endothelial cells. PMID: 21668763 a novel intronic splicing enhancer that regulates caspase 9 RNA splicing and specifically interacts with SRSF1 was identified. PMID: 21622622 negative regulation of the JC virus promoter by SF2/ASF may control reactivation of JCV replication in brain PMID: 21297941 phosphorylation of the RS domain in SRSF1 induces a key molecular switch from intra- to intermolecular interactions, suggesting a plausible mechanism for the documented requirement for the phosphorylation/dephosphorylation cycle during pre-mRNA splicing. PMID: 21536904

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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