Analytical Data
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Gene name
RPS2
- Application
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Alternative Names
PRMT3;HRMT1L3;Protein arginine N-methyltransferase 3
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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
P15880
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Expression Region
1-293aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMADDAGA AGGPGGPGGP GMGNRGGFRG GFGSGIRGRG RGRGRGRGRG RGARGGKAED KEWMPVTKLG RLVKDMKIKS LEEIYLFSLP IKESEIIDFF LGASLKDEVL KIMPVQKQTR AGQRTRFKAF VAIGDYNGHV GLGVKCSKEV ATAIRGAIIL AKLSIVPVRR GYWGNKIGKP HTVPCKVTGR CGSVLVRLIP APRGTGIVSA PVPKKLLMMA GIDDCYTSAR GCTATLGNFA KATFDAISKT YSYLTPDLWK ETVFTKSPYQ EFTDHLVKTH TRVSVQRTQA PAVATT
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Molecular Weight
34 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
RPS2, a member of the ribosomal protein family, plays a crucial role in ribosome biogenesis and the modulation of various cellular processes. It is integral to the assembly and function of the ribosomal machinery, which is essential for protein synthesis in all living organisms. Studies have shown that RPS2 is involved in various physiological and pathological processes, including cell growth, differentiation, and response to stress. Additionally, mutations or dysregulation of RPS2 have been implicated in diseases such as cancer, making it a potential target for therapeutic interventions. Recent advances in recombinant protein technology have facilitated the expression and purification of RPS2, enabling researchers to explore its structure-function relationship and interactions with other cellular components. By generating recombinant RPS2 proteins, scientists can investigate the molecular mechanisms underlying ribosome assembly and function, as well as examine how variations in RPS2 affect cellular homeostasis. This research is paving the way for a better understanding of ribosomal dynamics and its implications in health and disease, ultimately contributing to the development of novel strategies for disease treatment and management.
