Analytical Data
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Gene name
RGN
- Application
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Alternative Names
RGN;SMP30;Regucalcin
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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
Q15493
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Expression Region
1-299aa
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AA Sequence
MSSIKIECVL PENCRCGESP VWEEVSNSLL FVDIPAKKVC RWDSFTKQVQ RVTMDAPVSS VALRQSGGYV ATIGTKFCAL NWKEQSAVVL ATVDNDKKNN RFNDGKVDPA GRYFAGTMAE ETAPAVLERH QGALYSLFPD HHVKKYFDQV DISNGLDWSL DHKIFYYIDS LSYSVDAFDY DLQTGQISNR RSVYKLEKEE QIPDGMCIDA EGKLWVACYN GGRVIRLDPV TGKRLQTVKL PVDKTTSCCF GGKNYSEMYV TCARDGMDPE GLLRQPEAGG IFKITGLGVK GIAPYSYAG
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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
Recombinant proteins, like RGN (Regulator of G protein Signaling), have garnered significant attention in the field of biotechnology and molecular biology due to their vital roles in various cellular processes. RGN is known for its ability to modulate G protein signaling pathways, which are crucial for cellular communication, growth, and differentiation. Overexpression or manipulation of RGN can influence numerous physiological functions, thereby making it a potential target for therapeutic interventions in diseases such as cancer, heart disease, and neurological disorders. Advances in recombinant DNA technology have facilitated the production of RGN in host organisms like bacteria, yeast, and mammalian cells, allowing researchers to study its structure, function, and interactions in detail. Understanding the mechanisms by which RGN operates not only provides insights into fundamental biological processes but also informs the development of novel drugs and treatment strategies to enhance health outcomes. As research continues to unravel the complexities of G protein signaling and its association with various diseases, RGN stands out as a promising candidate for further investigation, with potential implications for clinical applications and therapeutic innovations.











