Recombinant Human Serine/Arginine-Rich Splicing Factor 3 (SRSF3) Protein (His-GB1)

Name: Recombinant Human Serine/Arginine-Rich Splicing Factor 3 (SRSF3) Protein (His-GB1)
Brand: Beta LifeScience
SKU: BLC-01649P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Serine/Arginine-Rich Splicing Factor 3 (SRSF3) Protein (His-GB1) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P84103
Target Symbol	SRSF3
Synonyms	Pre-mRNA-splicing factor SRP20;Splicing factor, arginine/serine-rich 3
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-GB1
Target Protein Sequence	MHRDSCPLDCKVYVGNLGNNGNKTELERAFGYYGPLRSVWVARNPPGFAFVEFEDPRDAADAVRELDGRTLCGCRVRVELSNGEKR
Expression Range	1-86aa
Protein Length	partial
Mol. Weight	17.9 kDa
Research Area	Epigenetics And Nuclear Signaling
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	Splicing factor that specifically promotes exon-inclusion during alternative splicing. Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing. Also functions as export adapter involved in mRNA nuclear export. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. Involved in nuclear export of m6A-containing mRNAs via interaction with YTHDC1: interaction with YTHDC1 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export. RNA-binding is semi-sequence specific.
Subcellular Location	Nucleus. Nucleus speckle. Cytoplasm.
Protein Families	Splicing factor SR family
Database References	HGNC: 10785 OMIM: 603364 KEGG: hsa:6428 STRING: 9606.ENSP00000362820 UniGene: PMID: 29857020 TDP43 alters most splicing events with splicing factor SRSF3 in triple-negative breast cancer. PMID: 29581274 Loss of SRSF3 expression was significantly associated with poor survival and shorter disease-free survival, particularly in early stages, in colorectal cancer. PMID: 29131639 Findings reveal the molecular mechanism of SRSF3 in pri-miRNA processing and support the previously proposed explanation for the highly conserved position of CNNC in SRSF3-enhanced pri-miRNA processing. PMID: 29615481 High expression of SRSF3 is associated with oral squamous cell carcinoma. PMID: 27808105 MicroRNA-1908-5p contributes to the oncogenic function of the splicing factor SRSF3 via NKIRAS2 axis in osteosarcoma cells. PMID: 28039456 Dehydroepiandrosterone (DHEA) and cortisol modulate SRSF9 and SRSF3 in a different way and data suggest that the anti-glucocorticoid effect of DHEA, among other mechanisms, is also exerted by modulating the expression of proteins involved in the splicing of the GR pre-mRNA. PMID: 28373129 that SRSF3 controls the expression of the miR-132/212 cluster through regulating REST expression PMID: 28624413 Alternative splicing of U2AF1 reveals a shared repression mechanism for duplicated exons controlled by SRF3. PMID: 27566151 Introduction of point mutations in the SRSF3-binding site or knockdown of SRSF3 expression in cells reduces human papillomavirus 18 929;3434 splicing and E1;E4 production but activates other, minor 929;3465 and 929;3506 splicing. Knockdown of SRSF3 expression also enhances the expression of E2 and L1 mRNAs. PMID: 27489271 data indicate that the Human Papillomavirus E2 protein links the viral replication cycle to epithelial differentiation via SRSF3, a key cellular regulator of high-risk (HR)-HPV gene expression PMID: 26962216 Results suggested that SRSF3 is associated with the initiation and development of OSCC and may be a biomarker and therapeutic target of OSCC. PMID: 27429590 we also demonstrated frequent co-overexpression and positive correlation of DARPP-32, SRp20 and CD44E expression levels in human gastric primary tumors. PMID: 26119931 Results show that YTHDC1 promotes exon inclusion in targeted mRNAs through recruiting pre-mRNA splicing factor SRSF3 while blocking SRSF10 mRNA binding. PMID: 26876937 These data indicate that SRSF3 affects a global change of gene expression to maintain cell homeostasis. PMID: 26704980 We propose that SRSF3 could act as a coordinator of the expression of PDCD4 protein via two mechanisms on two alternatively spliced mRNA isoforms. PMID: 26773498 This new function of SRSF3 not only explains why overexpression of SRSF3 is required for ovarian cancer cell growth and survival but also offers a new insight into the mechanism of the neoplastic transformation. PMID: 26282282 SRSF3 and hnRNP H1 are the first splicing factors identified which regulate the production of these functionally distinct HER2 splice variants and therefore maybe important for the regulation of HER2 signaling. PMID: 26367347 expression either decreased or the protein mislocalized in hepatocellular carcinoma PMID: 25132062 Results identified modulation of SRSF3 activity as the molecular mechanism by which ORF57 promotes RNA splicing. PMID: 25234929 Data suggest that the oncogenic potential of SRSF3 might be realized, in part, through the translational repression of PDCD4 mRNA. PMID: 24292556 Stress-inducible truncated SRSF3 may participate in the acceleration of cell growth through facilitating c-Jun-mediated G1 progression under stressful conditions. PMID: 24190040 This is the first study that demonstrates that rs1122608 confers protection against ischemic stroke and implicates splicing factor SFSR3 in the disease process PMID: 24190014 findings disclose an important role of SRSF3 in the regulation of the G1-to-S-phase progression and alternative splicing of HIPK2 in tumor growth PMID: 23503458 truncated SRSF3 protein may function as a positive regulator of oxidative stress-initiated inflammatory responses in colon cancer cells. PMID: 24284797 Therefore we conclude that SRSF3 promotes exon 9 skipping of caspase-2 pre-mRNA by interacting with exon 8 PMID: 24321384 Work described here examined the punctate pattern of SRp20 localization in the cytoplasm of poliovirus-infected cells, demonstrating the partial co-localization of SRp20 with the stress granule marker protein TIA-1. PMID: 23830997 Digoxin-mediated repression of SRSF3 expression plays a role in the digoxin-mediated inclusion of exon 20 in the IKBKAP transcript generated from the familial dysautonomia mutant allele. PMID: 23711097 downregulation of SRSF3 represents an endogenous mechanism for cellular senescence that directly regulates the TP53 alternative splicing to generate p53beta PMID: 22777358 results further define the mechanism of SRp20 cellular redistribution during picornavirus infections PMID: 23255796 Serine arginine splicing factor 3 is involved in enhanced splicing of glucose-6-phosphate dehydrogenase RNA in response to nutrients and hormones in liver PMID: 23233666 This study does not confirm a role for genetic variants in the SFRS3 and FKBP4 genes in the pathogenesis of corticosteroid-induced ocular hypertension. PMID: 22921020 This study found that significant changes in serine/arginine protein 20 (Srp20) gene expression in AD cases and confirmed this using a second cohort of control/AD. PMID: 22788679 Protein extracts of colon cancer CD133+ cell stem cells were compared to protein extracts of colon cancer cell CD133- stem cells by 2D DIGE. Demonstrated a direct cause-effect relationship between Wnt pathway activation & increased SRp20 expression. PMID: 22623141 Relative levels of SRp20, SRp30c, and SRp40 in TM cells control differential expression of the two alternatively spliced isoforms of the GR and thereby regulate GC responsiveness. PMID: 22205602 a model in which SRp20 interacts with PCBP2 bound to the viral RNA, and this interaction functions to recruit ribosomes to the viral RNA in a direct or indirect manner, with the participation of additional protein-protein or protein-RNA interactions. PMID: 21779168 Silencing of SFRS3 increased IL-1beta secretion due to elevation of IL-1beta and caspase-1 mRNA in addition to active caspase-1 levels. PMID: 21611201 expression of PTB and SRp20 is associated with malignancy of ovarian tumors but not with stage of invasive epithelial ovarian cancer PMID: 20856201 Results suggest that increased SRp20 expression in tumor cells is a critical step for tumor initiation, progression, and maintenance. PMID: 21179588 Epstein-Barr Virus SM protein utilizes cellular splicing factor SRp20 to mediate alternative splicing. PMID: 20810723 The authors report that siRNA knockdown of SRp20 or 9G8 resulted in about a 10 fold decrease in herpes simplex virus 1 yields and in nuclear accumulation of polyA+ RNA. PMID: 20227104 insulin induces the proteasome-dependent degradation of SRp20 as well as the subnuclear relocalization of CLIC1 PMID: 15827065 These results suggest that the C-terminal domain of RPB1 promotes exon skipping by recruiting SRp20 and that this contributes independently of elongation to the transcriptional control of alternative splicing. PMID: 17028590 nucleo-cytoplasmic SR protein, SRp20, functions in internal ribosome entry site (IRES)-mediated translation of a viral RNA. PMID: 17183366 abundant SRp20 in cancer cells or undifferentiated keratinocytes is important for the expression of the viral early E6 and E7 by promoting the expression of cellular transcription factor SP1 for transactivation of viral early promoters. PMID: 18945760 Study reports the splicing factor SRp20 as a novel target gene of beta-catenin/TCF4 signaling. PMID: 18952824 SRp20, SF2/ASF, and CUG-BP1 act antagonistically to regulate IR alternative splicing in vivo and that the relative ratios of SRp20 and SF2/ASF to CUG-BP1 in different cells determine the degree of exon inclusion. PMID: 19047369 SRp20 associate with interphase chromatin, and is released from hyperphosphorylated mitotic chromosomes PMID: 19250906

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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.

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