Analytical Data
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Gene name
SFRS17A
- Application
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Alternative Names
A-kinase anchor protein 17A. AKAP-17A. 721P. B-lymphocyte antigen. Protein XE7. Protein kinase A-anchoring protein 17A. PRKA17A. Splicing factor. arginine/serine-rich 17A
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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
Q02040
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Expression Region
1-446 aa
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AA Sequence
MAAATIVHDTSEAVELCPAYGLYLKPITKMTISVALPQLKQPGKSISNWEVMERLKGMVQNHQFSTLRISKSTMDFIRFEGEVENKSLVKSFLACLDGKTIKLSGFSDILKVRAAEFKIDFPTRHDWDSFFRDAKDMNETLPGERPDTIHLEGLPCKWFALKESGSEKPSEDVLVKVFEKFGEIRNVDIPMLDSYREEMTGRNFHTFSFGGHLNFEAYVQYREYMGFIQAMSALRGMKLMYKGEDGKAVACNIKVSFDSTKHLSDASIKKRQLERQKLQELEQQREEQKRREKEAEERQRAEERKQKELEELERERKREEKLRKREQKQRDRELRRNQKKLEKLQAEEQKQLQEKIKLEERKLLLAQRNLQSIRLIAELLSRAKVPGGSLCSRQPRPGCPQCPPLKCGRRHGAVSPPAAAVATKPALMPRMTAPSREGVALVCRSR
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Molecular Weight
74.8 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
The SFRS17A protein, a member of the splicing factor family, has gained significant attention in recent years due to its pivotal role in pre-mRNA splicing and gene regulation. Emerging evidence suggests that SFRS17A is not only involved in the standard splicing process but also plays a critical role in alternative splicing, which can greatly influence protein diversity and cellular function. Studies have shown that dysregulation of splicing factors, including SFRS17A, is implicated in various diseases, particularly cancers and neurodegenerative disorders. Furthermore, SFRS17A has been associated with the progression of certain malignancies, making it a potential biomarker for diagnosis and prognosis. The exploration of SFRS17A's structure and function, as well as its interactions with other splicing regulators and RNA molecules, is essential for understanding its biological significance and therapeutic potential. Given the intricate networks of gene regulation and the impact of splicing on cellular homeostasis, research into SFRS17A could uncover novel insights into molecular mechanisms underlying disease states and offer opportunities for targeted interventions. Thus, the ongoing investigation into SFRS17A and its role in splicing highlights the intersection of molecular biology, genetics, and potential clinical applications.
