Analytical Data
-
Gene name
PUS1
- Application
-
Alternative Names
PUS1;Pseudouridylate synthase 1 homolog
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y606
-
Expression Region
1-427aa
-
AA Sequence
MGLQLRALLGAFGRWTLRLGPRPSCSPRMAGNAEPPPAGAACPQDRRSCSGRAGGDRVWEDGEHPAKKLKSGGDEERREKPPKRKIVLLMAYSGKGYHGMQRNVGSSQFKTIEDDLVSALVRSGCIPENHGEDMRKMSFQRCARTDKGVSAAGQVVSLKVWLIDDILEKINSHLPSHIRILGLKRVTGGFNSKNRCDARTYCYLLPTFAFAHKDRDVQDETYRLSAETLQQVNRLLACYKGTHNFHNFTSQKGPQDPSACRYILEMYCEEPFVREGLEFAVIRVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGTEKVDVPKAPGLGLVLERVHFEKYNQRFGNDGLHEPLDWAQEEGKVAAFKEEHIYPTIIGTERDERSMAQWLSTLPIHNFSATALTAGGTGAKVPSPLEGSEGDGDTD
-
Molecular Weight
47.4 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
PUS1, or pseudouridine synthase 1, is an enzyme that plays a vital role in the post-transcriptional modification of RNA, specifically the conversion of uridine to pseudouridine. This modification is crucial for the stability and functionality of various RNA molecules, including tRNA, rRNA, and snRNA. Research on PUS1 has gained momentum due to its implications in multiple biological processes and diseases. Abnormalities in PUS1 activity have been linked to disorders such as cancer and neurodegeneration, making it a potential target for therapeutic intervention. Additionally, PUS1 is involved in the regulation of gene expression and the maintenance of cellular homeostasis. Understanding the structure and function of PUS1, as well as its interaction with RNA substrates, can provide insights into the molecular mechanisms underlying its role in RNA biology. Researchers have been employing recombinant protein techniques to produce PUS1, facilitating detailed studies of its enzymatic activity and substrate specificity. This research not only enhances our understanding of RNA modifications but also opens avenues for discovering novel therapeutic strategies that leverage the manipulation of PUS1 activity in various diseases. The growing interest in PUS1 underscores its significance in the field of molecular biology and its potential as a biomarker or therapeutic target in the treatment of RNA-related diseases.











