Analytical Data
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Gene name
TPSg1
- Application
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Alternative Names
TMT; PRSS31; Tryptase Gamma II; Tryptase Gamma I; Serine protease 31; Transmembrane tryptase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NRR2
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Expression Region
Thr99~Glu244
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Molecular Weight
20kDa
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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
TPSg1, a recombinant protein derived from specific plant or microbial sources, has garnered significant interest in the field of biochemistry and biotechnology due to its potential applications in various industries, including agriculture, food technology, and pharmaceuticals. This protein is particularly noted for its role in metabolic pathways, influencing processes such as stress response and growth regulation in organisms. Research into TPSg1 focuses on its structural properties, functional mechanisms, and interactions within biological systems. Understanding the molecular characteristics of TPSg1 can lead to innovative applications, such as enhancing crop resilience to environmental stressors or developing novel therapeutic agents. The advances in recombinant DNA technology have enabled researchers to produce TPSg1 in significant quantities, facilitating detailed studies of its biochemical activities and potential therapeutic uses. As an example, its recombinant forms have been explored for their benefits in improving plant resistance to diseases or pests, which aligns with the growing need for sustainable agricultural practices. Furthermore, the insights gained from TPSg1 research may also contribute to the development of bioactive compounds with medicinal properties, highlighting the multifaceted importance of this protein in both basic and applied science. Overall, the ongoing exploration of TPSg1 promises to unlock new avenues for enhancing biotechnology applications and advancing our understanding of protein functionality in diverse biological contexts.
