Analytical Data
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Gene name
SRSF2
- Application
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Alternative Names
SFRS2; PR264; SC-35; SC35; SFRS2A; SRp30b; Splicing component, 35 kDa; Splicing factor, arginine/serine-rich 2
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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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
Thr14~Ser221
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Molecular Weight
54&50&44kDa
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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
SRSF2 (Serine/Arginine-rich splicing factor 2) is a crucial RNA-binding protein that plays a significant role in the regulation of pre-mRNA splicing and has been implicated in various cellular processes, including gene expression and mRNA processing. Recent studies have highlighted its involvement in cancer biology, particularly in acute myeloid leukemia (AML), where mutations in SRSF2 have been linked to disease progression and poor prognosis. These mutations often cause aberrant splicing patterns, leading to the production of oncogenic isoforms that contribute to tumorigenesis. Given its pivotal role in splicing regulation, SRSF2 has emerged as a potential therapeutic target, prompting researchers to explore the functional consequences of its mutations and the mechanisms by which they alter splicing dynamics. Understanding the structure and function of SRSF2 is crucial for elucidating its role in cancer and for developing novel splicing-modulating therapies. Therefore, the recombinant expression and purification of SRSF2 protein are essential steps in investigating its biochemical properties, binding interactions, and the effects of specific mutations, thereby advancing our knowledge of its contribution to splicing regulation and cancer pathogenesis.
