Analytical Data
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Gene name
RPUSD1
- Application
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Alternative Names
RPUSD1; C16orf40; RLUCL; RNA pseudouridylate synthase domain-containing protein 1; Ribosomal large subunit pseudouridine synthase C-like protein
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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
Q9UJJ7
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Expression Region
1-312 aa
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AA Sequence
MEPGSVENLS IVYRSRDFLV VNKHWDVRID SKAWRETLTL QKQLRYRFPE LADPDTCYGF RFCHQLDFST SGALCVALNK AAAGSAYRCF KERRVTKAYL ALLRGHIQES RVTISHAIGR NSTEGRAHTM CIEGSQGCEN PKPSLTDLVV LEHGLYAGDP VSKVLLKPLT GRTHQLRVHC SALGHPVVGD LTYGEVSGRE DRPFRMMLHA FYLRIPTDTE CVEVCTPDPF LPSLDACWSP HTLLQSLDQL VQALRATPDP DPEDRGPRPG SPSALLPGPG RPPPPPTKPP ETEAQRGPCL QWLSEWTLEP DS
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Molecular Weight
34.7 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
RPUSD1, or RNA pseudouridylate synthase 1, is an essential enzyme involved in post-transcriptional RNA modification, specifically the conversion of uridine to pseudouridine in various RNA molecules. This modification plays a significant role in the stability, structure, and function of RNA, impacting gene expression and cellular processes. Research into RPUSD1 has gained momentum due to its association with several human diseases and its potential role in cancer biology, where altered RNA modifications can lead to aberrant cell signaling and tumor progression. Understanding the structural and functional mechanisms of RPUSD1 through recombinant protein studies enables researchers to dissect its enzymatic function and regulatory networks. With advances in biophysical techniques and molecular biology, the characterization of RPUSD1 not only aids in comprehending fundamental biological processes but may also reveal novel therapeutic targets for conditions linked to dysregulated RNA modifications. As such, RPUSD1 is positioned at the intersection of RNA biology, disease mechanisms, and therapeutic innovation, making it a compelling focus for ongoing research in both basic and applied sciences.
