Analytical Data
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Gene name
SFRS2
- Application
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Alternative Names
35 kDa; arginine/serine-rich 2; PR264; Protein PR264; SC 35; SC-35; SC35; Serine/arginine-rich splicing factor 2; SFRS 2; SFRS2; SFRS2A; Splicing component 35 kDa; Splicing component; Splicing factor; Splicing factor arginine/serine rich 2; Splicing factor SC35; Splicing speckle; Splicing speckles; SR splicing factor 2; SRp30b; SRSF2; SRSF2_HUMAN
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q01130
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Expression Region
1-179 aa
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AA Sequence
MSYGRPPPDVEGMTSLKVDNLTYRTSPDTLRRVFEKYGRVGDVYIPRDRYTKESRGFAFVRFHDKRDAEDAMDAMDGADPGVGAVPGLAADLATAARSLGPALVLDLGRPPSPDPHEGPSPSPRRSPDLVRGPGPGLGPGVLPQCPRGNPNPGRDRRVPPSLLKRKERCPLKKMLRSPV
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Molecular Weight
45.43 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
SFRS2, or Serine/Arginine-rich splicing factor 2, is a critical protein involved in the regulation of pre-mRNA splicing, a fundamental process that influences gene expression and protein diversity. Dysregulation of splicing factors like SFRS2 has been implicated in various diseases, including cancers and neurodegenerative disorders. Research into SFRS2 has gained momentum due to its dual role in facilitating spliceosome assembly and its involvement in alternative splicing mechanisms. Studies have shown that SFRS2 can influence the splicing isoforms of key oncogenes and tumor suppressor genes, thereby impacting cellular proliferation and survival. Additionally, SFRS2's interactions with other splicing factors and cellular proteins highlight its importance in the broader network of gene regulation. Understanding the structure, function, and regulatory mechanisms of SFRS2 is crucial for elucidating its role in health and disease. Recent advancements in protein engineering and molecular biology techniques have opened new avenues for the study of SFRS2, providing insights that may lead to the development of novel therapeutic strategies targeting splicing aberrations associated with various pathologies. Thus, investigating SFRS2 and its corresponding recombinant proteins holds significant promise for both basic research and clinical applications in the field of molecular medicine.
