Analytical Data
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Gene name
TPST2
- Application
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Alternative Names
Tyrosylprotein sulfotransferase 2 ;TPST-2
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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
O60704
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Expression Region
26-377aa
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Molecular Weight
55.3 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
TPST2 (tyrosylprotein sulfotransferase 2) is an enzyme that plays a critical role in the sulfation of tyrosine residues on proteins, a post-translational modification that influences protein stability, activity, and interactions. The study of TPST2 has gained interest due to its potential implications in various biological processes and diseases, including cancer, where altered protein sulfation patterns can affect tumor growth and metastasis. Furthermore, TPST2 has been implicated in the regulation of immune responses and cellular signaling pathways. Understanding the structural and functional characteristics of TPST2 through recombinant protein studies can provide insights into its specific substrate recognition, catalytic mechanisms, and the broader impacts on cellular function. With the advancement of recombinant protein technology, researchers are able to produce and characterize TPST2 in vitro, paving the way for the exploration of its therapeutic potential and the development of specific inhibitors that could modulate its activity. This research is not only significant for basic biological understanding but also for potential clinical applications in targeted therapies for diseases associated with dysregulated sulfation processes.
