Analytical Data
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Gene name
THG1L
- Application
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Alternative Names
THG1L；ICF45；Probable tRNA(His) guanylyltransferase
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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
Q9NWX6
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Expression Region
30-298aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAKSKFE YVRDFEADDT CLAHCWVVVR LDGRNFHRFA EKHNFAKPND SRALQLMTKC AQTVMEELED IVIAYGQSDE YSFVFKRKTN WFKRRASKFM THVASQFASS YVFYWRDYFE DQPLLYPPGF DGRVVVYPSN QTLKDYLSWR QADCHINNLY NTVFWALIQQ SGLTPVQAQG RLQGTLAADK NEILFSEFNI NYNNELPMYR KGTVLIWQKV DEVMTKEIKL PTEMEGKKMA VTRTRTKPVP LHCDIIGDAF WKEHPEILDE DS
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Molecular Weight
34 kD
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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
THG1L (Thymidine Kinase 1-Like Protein) is an intriguing member of the thymidine kinase family, primarily known for its role in nucleotide metabolism. The research on THG1L has gained traction due to its emerging implications in various biological processes and diseases, including cancer and neurodegenerative disorders. Unlike classical thymidine kinases, THG1L is speculated to participate in RNA metabolism, potentially influencing cellular responses to stress and playing a role in the regulation of gene expression. Its unique structure and enzymatic properties suggest that it may serve as a critical player in the balance between cell proliferation and apoptosis. By studying the recombinant form of THG1L, researchers aim to elucidate its functional mechanisms and interactions within the cell. Understanding THG1L's role is crucial for developing targeted therapeutics and advancing our knowledge of cellular biology, particularly in the context of tumorigenesis and cellular aging. The recombinant protein presents opportunities for structural biology studies, enzyme kinetics, and drug design, laying the groundwork for future research that may uncover novel therapeutic strategies leveraging THG1L's biochemical pathways. Overall, the investigation into THG1L's recombinant protein not only highlights its potential significance in health and disease but also opens avenues for innovative approaches in biomedical research.
