Analytical Data
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Gene name
SRSF4
- Application
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Alternative Names
SRSF4；SFRS4；SRP75；Serine/arginine-rich splicing factor 4
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Species
Mouse
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8VE97
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Expression Region
1-489aa
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AA Sequence
MPRVYIGRLS YQARERDVER FFKGYGKILE VDLKNGYGFV EFDDLRDADD AVYELNGKDL CGERVIVEHA RGPRRDGSYG SGRSGYGYRR SGRDKYGPPT RTEYRLIVEN LSSRCSWQDL KDYMRQAGEV TYADAHKGRK NEGVIEFVSY SDMKRALEKL DGTEVNGRKI RLVEDKPGSR RRRSYSRSRS HSRSRSRSRH SRKSRSRSGS SKSSHSKSRS RSRSGSHSRS KSRSRSQSRS RSKKEKSRSP SKDNKSRSRS RSPDKSRSKS KDHAEDKLQN NDSAGKAKSH SPSRHDSKSR SRSQERRAEE ERRRSVSRAR SQEKSRSQEK SLLKSRSRSR SRSRSRSKDK RKGRKRSRDE SRSRSRSKSE RSRKHSSKRD SKVSSSSSSS KKKKDTDHSR SPSRSVSKER EHAKAESGQR GSRAEGESEA PNPEPRARSR STSKSKPNVP AESRSRSKSA SKTRSRSKSP SRSASRSPSR SRSRSHSRS
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Molecular Weight
55.9 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
SRSF4, a member of the serine/arginine-rich splicing factor family, plays a critical role in the regulation of mRNA splicing and is involved in various cellular processes including gene expression and cell signaling. Its significance has been increasingly recognized in the context of cancer biology, where abnormal splicing patterns can contribute to tumorigenesis and malignant progression. Research has shown that SRSF4 can affect the splicing of pre-mRNAs that encode proteins involved in cell growth, apoptosis, and differentiation, making it a potential biomarker and therapeutic target. Furthermore, SRSF4 interacts with a variety of splicing machinery components and is modulated by several signaling pathways, indicating its complex involvement in cellular homeostasis. Studies have also suggested that the dysregulation of SRSF4 expression may lead to the development of distinct cancer phenotypes, as aberrant splicing events can generate oncogenic isoforms. Understanding the functional mechanisms and regulatory pathways of SRSF4 is essential for elucidating its role in cancer pathology and can provide insights into the development of innovative therapeutic strategies targeting splicing dysregulation in various malignancies. Thus, the investigation of SRSF4 recombinant proteins is crucial for exploring its diverse functions and for developing SRSF4-targeted interventions in cancer treatment.
