Analytical Data
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Gene name
SRRM2
- Application
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Alternative Names
300 kDa nuclear matrix antigen (Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa) (SR-related nuclear matrix protein of 300 kDa) (Ser/Arg-related nuclear matrix protein of 300 kDa) (Splicing coactivator subunit SRm300) (Tax-responsive enhancer element-binding protein 803) (TaxREB803) (KIAA0324) (SRL300) (SRM300)
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Species
Human
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Source
Baculovirus
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UQ35
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Expression Region
1666-2089aa
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Molecular Weight
53.8 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
SRRM2, or Serine/Arginine Rich Splicing Factor 2, is a critical protein involved in the regulation of mRNA splicing processes, affecting gene expression and cellular function. As a member of the serine/arginine-rich (SR) proteins family, SRRM2 plays a pivotal role in spliceosome assembly and the selection of splice sites, thereby influencing the generation of diverse mRNA isoforms. Research on SRRM2 has gained significance due to its implications in various biological processes, including cell differentiation, proliferation, and the response to cellular stress. Dysregulation of SRRM2 has been linked to several diseases, particularly cancer, where altered splicing patterns contribute to tumorigenesis and cancer progression. Moreover, studies have shown that SRRM2 interacts with other splicing factors and can modulate the expression of genes involved in critical pathways, making it a potential target for therapeutic interventions. Understanding the structural and functional aspects of SRRM2 through recombinant protein studies can provide insights into its role in splicing regulation and its impact on health and disease. This research is essential for uncovering the molecular mechanisms underlying SRRM2 function and for exploring its potential as a biomarker or therapeutic target in diseases associated with splicing dysregulation.
