Analytical Data
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Gene name
RNPS1
- Application
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Alternative Names
E5.1; MGC117332; RNA binding protein S1 serine rich domain; RNA binding protein with serine rich domain 1; RNA-binding protein with serine-rich domain 1; RNPS 1; rnps1; RNPS1_HUMAN; SR protein; SR related protein LDC2; SR-related protein LDC2
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Species
Human
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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
Q15287
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Expression Region
1-305 aa
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AA Sequence
MDLSGVKKKS LLGVKENNKK SSTRAPSPTK RKDRSDEKSK DRSKDKGATK ESSEKDRGRD KTRKRRSASS GSSSTRSRSS STSSSGSSTS TGSSSGSSSS SASSRSGSSS TSRSSSSSSS SGSPSPSRRR HDNRRRSRSK SKPPKRDEKE RKRRSPSPKP TKVHIGRLTR NVTKDHIMEI FSTYGKIKMI DMPVERMHPH LSKGYAYVEF ENPDEAEKAL KHMDGGQIDG QEITATAVLA PWPRPPPRRF SPPRRMLPPP PMWRRSPPRM RRRSRSPRRR SPVRRRSRSP GRRRHRSRSS SNSSR
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Molecular Weight
34.2 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
RNPS1, or RNA-binding protein with serine-rich domain 1, has emerged as a significant focus in molecular biology and cancer research due to its involvement in crucial cellular processes such as RNA splicing, transport, and degradation. As a key regulator of gene expression, RNPS1 interacts with various RNA molecules, playing a pivotal role in maintaining cellular homeostasis. Recent studies have highlighted its potential implications in tumorigenesis, with overexpression linked to aggressive cancer phenotypes. Understanding the structure and function of RNPS1 through recombinant protein studies can provide insights into its mechanism of action and regulatory roles in oncogenic pathways. Furthermore, RNPS1 is also associated with cellular stress responses, making it a potential target for therapeutic interventions. Investigating RNPS1 as a recombinant protein opens avenues for developing inhibitors or modulators that could alter its activity, offering promising strategies for cancer treatment and the management of related diseases. As research progresses, unraveling the complexities of RNPS1 may lead to novel biomarkers and therapeutic targets, enhancing our ability to combat various malignancies.
