Analytical Data
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Gene name
SRPK2
- Application
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Alternative Names
SFRSK2; SFRS Protein Kinase 2; Serine/arginine-rich protein-specific kinase 2
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P78362
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Expression Region
Glu380~Leu617
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Molecular Weight
40kDa
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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
SRPK2 (Serine/Arginine-rich protein kinase 2) is a crucial member of the SR protein kinase family, which plays a significant role in the phosphorylation of serine/arginine-rich splicing factors, thereby modulating pre-mRNA splicing and influencing gene expression. The importance of SRPK2 has been highlighted in various biological processes, including cell proliferation, differentiation, and response to stress. Dysregulation of SRPK2 has been implicated in several diseases, particularly cancer, where altered splicing patterns can lead to tumor progression and metastasis. Moreover, understanding the precise mechanisms by which SRPK2 regulates splicing has significant implications for therapeutic strategies targeting splicing-related pathologies. In recent years, there has been growing interest in the recombinant production of SRPK2 to facilitate biochemical studies aimed at uncovering its functional roles and regulatory mechanisms. The generation of recombinant SRPK2 proteins allows for detailed analyses of its kinase activity, substrate specificity, and interaction with splicing factors. Such studies are essential for elucidating the complex regulatory networks involving SRPK2, providing insights that could lead to novel diagnostic or therapeutic approaches in diseases linked to splicing abnormalities. As research continues to expand, the investigation of SRPK2 through recombinant protein technology remains a promising avenue for uncovering its potential as a target in the development of splicing-focused therapies.
