Recombinant Human Serine/Arginine-Rich Splicing Factor 10 (SRSF10) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-10488P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) SRSF10.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) SRSF10.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) SRSF10.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) SRSF10.

Recombinant Human Serine/Arginine-Rich Splicing Factor 10 (SRSF10) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-10488P
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Product Overview

Description Recombinant Human Serine/Arginine-Rich Splicing Factor 10 (SRSF10) 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 O75494
Target Symbol SRSF10
Synonyms 40 kDa SR repressor protein; 40 kDa SR-repressor protein; Anti TLS associated protein with SR repeats; arginine/serine-rich 13A; FUS interacting protein serine arginine rich 1; FUS interacting protein serine arginine rich 2; FUS interacting serine arginine rich protein 1; FUS-interacting serine-arginine-rich protein 1; FUSIP1; FUSIP2; NSSR; OTTHUMP00000015774; Serine arginine repressor protein 40 kDa; Serine/arginine-rich splicing factor 10; SFRS13; SFRS13A; Splicing factor; Splicing factor arginine serine rich 13; Splicing factor SRp38; SRp38; SRp40; SRrp40; SRS10_HUMAN; Srsf10; TASR; TASR1; TASR2; TLS associated protein TASR1; TLS associated protein TASR2; TLS associated protein with Ser Arg repeats; TLS associated protein with SR repeats; TLS associated serine arginine protein 1; TLS associated serine arginine protein 2; TLS associated serine arginine protein; TLS associated SR protein; TLS-associated protein with Ser-Arg repeats; TLS-associated protein with SR repeats; TLS-associated serine-arginine protein; TLS-associated SR protein
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence MSRYLRPPNTSLFVRNVADDTRSEDLRREFGRYGPIVDVYVPLDFYTRRPRGFAYVQFEDVRDAEDALHNLDRKWICGRQIEIQFAQGDRKTPNQMKAKEGRNVYSSSRYDDYDRYRRSRSRSYERRRSRSRSFDYNYRRSYSPRNSRPTGRPRRSRSHSDNDRPNCSWNTQYSSAYYTSRKI
Expression Range 1-183aa
Protein Length Full Length of Isoform 3
Mol. Weight 38.2kDa
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 in its dephosphorylated form acts as a general repressor of pre-mRNA splicing. Seems to interfere with the U1 snRNP 5'-splice recognition of SNRNP70. Required for splicing repression in M-phase cells and after heat shock. Also acts as a splicing factor that specifically promotes exon skipping during alternative splicing. Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing. May be involved in regulation of alternative splicing in neurons, with isoform 1 acting as a positive and isoform 3 as a negative regulator.
Subcellular Location Nucleus speckle. Cytoplasm.
Protein Families Splicing factor SR family
Database References

HGNC: 16713

OMIM: 605221

KEGG: hsa:10772

STRING: 9606.ENSP00000420195

UniGene: PMID: 27851963

  • Results show that YTHDC1 promotes exon inclusion in targeted mRNAs through recruiting pre-mRNA splicing factor SRSF3 while blocking SRSF10 mRNA binding. PMID: 26876937
  • SRSF10 is a key regulator of BCLAF1 pre-mRNA splicing and the maintenance of oncogenic features in human colon cancer cells PMID: 25091051
  • In colorectal cancer, NSSR1 was highly expressed in the nucleus of tumor cells. PMID: 21984158
  • Splicing thermotolerance is acquired through maintenance of SRSF10 phosphorylation and that this is mediated at least in part by Hsp27. PMID: 21135127
  • Data show that SFRS13A expression was significantly associated with LDLR splicing efficiency in vivo. PMID: 20232416
  • found to be dephosphorylated specifically in mitotic cells; show that dephosphorylated SRp38 is required for the observed splicing repression PMID: 12419250
  • SRp38 plays a crucial role in cell survival under stress conditions by inhibiting the splicing machinery PMID: 14765198
  • SRp38 contains two arginine- and serine-rich domains (RS), one of which has a unique, second-step repression activity, while both function together as a splicing repression domain. PMID: 16135820
  • FAQs

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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.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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