Analytical Data
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Gene name
PSR
- Application
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Alternative Names
JMJD6;KIAA0585;PSR;PTDSR;Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6
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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
Q6NYC1-3
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Expression Region
1-414aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNHKSKK RIREAKRSAR PELKDSLDWT RHNYYESFSL SPAAVADNVE RADALQLSVE EFVERYERPY KPVVLLNAQE GWSAQEKWTL ERLKRKYRNQ KFKCGEDNDG YSVKMKMKYY IEYMESTRDD SPLYIFDSSY GEHPKRRKLL EDYKVPKFFT DDLFQYAGEK RRPPYRWFVM GPPRSGTGIH IDPLGTSAWN ALVQGHKRWC LFPTSTPREL IKVTRDEGGN QQDEAITWFN VIYPRTQLPT WPPEFKPLEI LQKPGETVFV PGGWWHVVLN LDTTIAITQN FASSTNFPVV WHKTVRGRPK LSRKWYRILK QEHPELAVLA DSVDLQESTG IASDSSSDSS SSSSSSSSDS DSECESGSEG DGTVHRRKKR RTCSMVGNGD TTSQDDCVSK ERSSSRIRDT CGGRAHP
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Molecular Weight
50 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
Related Products
Protein Description
The study of PSR (proline-stabilized ring) proteins has garnered significant interest in recent years due to their unique structural and functional properties. PSR proteins are characterized by their ability to maintain stability in harsh environmental conditions, which is primarily attributed to the presence of proline residues that confer resilience to thermal denaturation and oxidative stress. These proteins are often found in extremophiles, organisms that thrive in extreme environments, such as high temperatures or salinities, making them valuable for biotechnological applications. Research into PSR proteins seeks to elucidate their roles in cellular processes, such as protein folding, stress response, and metabolism. Understanding the mechanisms underlying their stability and function can provide insights into evolutionary adaptations and facilitate the design of engineered proteins with enhanced stability for industrial and pharmaceutical applications. Additionally, the potential of PSR proteins as biomarkers for environmental stress responses presents opportunities for ecological and environmental monitoring. Ongoing studies aim to characterize the structural features of PSR proteins further and explore their applications in diverse fields, including biotechnology, medicine, and environmental science.
