Analytical Data
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Gene name
TPS
- Application
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Alternative Names
TPS；Protein-tyrosine sulfotransferase 2
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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
O60704
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Expression Region
1-377aa
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AA Sequence
MRLSVRRVLLAAGCALVLVLAVQLGQQVLECRAVLAGLRSPRGAMRPEQEELVMVGTNHVEYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWSKSGREKLRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLSRLFPNSKFLLMVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGKEKCLPVYYEQLVLHPRRSLKLILDFLGIAWSDAVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSKWTGHIPGDVVRDMAQIAPMLAQLGYDPYANPPNYGNPDPFVINNTQRVLKGDYKTPANLKGYFQVNQNSTSSHLGSS
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Molecular Weight
41.9 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
The study of TPS (trehalose-6-phosphate synthase) recombinant proteins has garnered significant attention in recent years due to their pivotal role in regulating trehalose metabolism, a crucial sugar involved in various biological processes. Trehalose plays an essential part in stress resistance, energy metabolism, and cellular signaling across a range of organisms, from bacteria to higher plants and animals. Understanding TPS is particularly important because it aids in the adaptation of cells to environmental stresses such as drought, heat, and salinity, making it valuable for agricultural applications. Additionally, TPS is involved in numerous metabolic pathways, influencing growth and development in organisms. Advances in biotechnology have enabled the production of recombinant TPS proteins, allowing researchers to explore their structural and functional properties in detail. By employing techniques such as gene cloning, expression in heterologous systems, and biochemical characterization, scientists can investigate the enzyme's mechanism of action, regulation, and interaction with other metabolic pathways. These insights not only enhance our understanding of basic metabolic functions but also open avenues for developing genetically engineered crops with improved resilience and yield. Furthermore, TPS's potential implications in biomedicine, particularly in the context of neurodegenerative diseases and cellular stress responses, underscore its significance. Thus, TPS recombinant protein research stands at the intersection of fundamental biology and applied science, driving innovations in crop science and therapeutic strategies.
