Analytical Data
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Gene name
TGS1
- Application
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Alternative Names
CLL-associated antigen KW-2;Cap-specific guanine-N2 methyltransferaseHepatocellular carcinoma-associated antigen 137Nuclear receptor coactivator 6-interacting protein;PRIP-interacting protein with methyltransferase motif ;PIMT ;PIPMT
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96RS0
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Expression Region
713-853aa
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Molecular Weight
31.6 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
TGS1 (Next-generation RNA 7-methylguanylate cap binding protein 1) is a key player in the regulation of gene expression, specifically in the context of mRNA stability and translation. Research on TGS1 has gained significant attention due to its crucial role in the 5' cap modification of RNA molecules, which is essential for mRNA processing, enhancing translation efficiency, and protecting mRNA from degradation. TGS1 is known to interact with the cap structure of mRNAs, facilitating their localization and stability within the cell. Disruptions in the functioning of TGS1 have been associated with various diseases, including cancer, where altered RNA metabolism plays a critical role in tumorigenesis. Therefore, understanding the biochemical properties and biological functions of TGS1 not only provides insights into fundamental cellular processes but also presents potential therapeutic targets for interventions in RNA-related diseases. Recent advances in structural biology techniques, such as X-ray crystallography and cryo-electron microscopy, have allowed researchers to elucidate the three-dimensional structure of TGS1, shedding light on its interaction mechanisms at the molecular level. As we delve deeper into the functional implications of TGS1 through biochemical assays and genetic studies, the ongoing research aims to uncover novel regulatory pathways and contribute to the development of RNA-targeted therapies, making TGS1 a significant focus in the realm of molecular biology and medicine.
