Analytical Data
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Gene name
PSTK
- Application
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Alternative Names
PSTK; C10orf89; L-seryl-tRNA(Sec) kinase; EC 2.7.1.164; O-phosphoseryl-tRNA(Sec) kinase
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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
Q8IV42
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Expression Region
1-348 aa
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AA Sequence
MKTAENIRGT GSDGPRKRGL CVLCGLPAAG KSTFARALAH RLQQEQGWAI GVVAYDDVMP DAFLAGARAR PAPSQWKLLR QELLKYLEYF LMAVINGCQM SVPPNRTEAM WEDFITCLKD QDLIFSAAFE AQSCYLLTKT AVSRPLFLVL DDNFYYQSMR YEVYQLARKY SLGFCQLFLD CPLETCLQRN GQRPQALPPE TIHLMGRKLE KPNPEKNAWE HNSLTIPSPA CASEASLEVT DLLLTALENP VKYAEDNMEQ KDTDRIICST NILHKTDQTL RRIVSQTMKE AKGNQEAFSE MTFKQRWVRA NHAAIWRIIL GNEHIKCRSA KVGWLQCCRI EKRPLSTG
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Molecular Weight
39.5 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
PSTK (Phosphoseryl-tRNA Kinase) is a key enzyme involved in the post-transcriptional modification of tRNA, specifically in the phosphorylation of serine residues on tRNA molecules. This process is crucial for the proper functioning of tRNA as it influences amino acid charging and the overall efficiency of protein synthesis. The interest in PSTK and its role in cellular processes has surged in recent years, driven by the growing understanding of the significance of tRNA modifications in cellular homeostasis, stress responses, and disease conditions. Abnormalities in tRNA modifications have been linked to various diseases, including neurodegenerative disorders and cancer, making PSTK a potential target for therapeutic interventions. Research into PSTK's structure, mechanism, and regulation offers insights into its contribution to the translation machinery and highlights its potential as a biomarker or drug target. Furthermore, advancements in techniques such as mass spectrometry and cryo-electron microscopy have facilitated a deeper exploration of PSTK functions, encouraging interdisciplinary studies that encompass biochemistry, molecular biology, and biomedical research. Understanding PSTK and its role in the modification of tRNA not only enriches the fundamental knowledge of genetic expression and regulation but also paves the way for developing novel therapeutic strategies aimed at diseases where tRNA modifications play a pivotal role.











