Analytical Data
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Gene name
LqhaIT
- Application
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Alternative Names
Lqh-alpha-IT Short name: Alpha-IT
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Species
Leiurus quinquestriatus
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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
P17728
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Expression Region
20-85aa
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Molecular Weight
23.5 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 LqhaIT recombinant protein has emerged as a significant focus in the fields of biotechnology and medicine, particularly due to its potential applications in therapeutic interventions and vaccine development. LqhaIT is derived from the Lqha species, which exhibits unique biochemical properties that make it an attractive candidate for various biomedical applications. Researchers are particularly interested in its role in modulating immune responses, as well as its potential use in targeted drug delivery systems. Advances in recombinant DNA technology have facilitated the production of LqhaIT in various expression systems, allowing for detailed investigation of its structure and function. Understanding the molecular mechanisms by which LqhaIT interacts with biological systems can pave the way for innovative treatments for a wide range of diseases, including autoimmune disorders and cancer. This research is further bolstered by the growing demand for effective biopharmaceuticals that can be engineered to elicit specific biological activities. Consequently, ongoing studies aim to elucidate the optimal conditions for LqhaIT expression, purification, and functional characterization, with the ultimate goal of harnessing its therapeutic potential. The convergence of molecular biology, immunology, and bioengineering in the research of LqhaIT underscores its critical importance in the development of next-generation biotechnological solutions.
