Analytical Data
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Gene name
KTx
- Application
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Alternative Names
Toxin Vm24 Toxin alpha-KTx 21.1
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Species
Vaejovis mexicanus smithi
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Source
HEK293
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0DJ31
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Expression Region
1-36aa
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Molecular Weight
7.9 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
Related Products
Protein Description
KTx recombinant proteins are a focus of extensive research due to their potential applications in various fields, including medicine and biotechnology. KTx, or potassium channel toxins, are naturally occurring peptides found in the venom of certain species of spiders and scorpions. These toxins exhibit a high degree of specificity for different types of potassium channels, making them valuable tools for studying ion channel biology and function. The ability to produce KTx proteins through recombinant DNA technology allows researchers to analyze their structure and function in a controlled environment, facilitating insights into their mechanisms of action. Furthermore, the specific interactions between KTx toxins and potassium channels can aid in the development of novel therapeutics for conditions related to ion channel dysfunction, such as cardiac arrhythmias or neurological disorders. Additionally, understanding the evolutionary adaptations of these proteins can contribute to the field of drug design by identifying lead compounds for pharmaceutical development. As a result, the exploration of KTx recombinant proteins not only enhances our fundamental knowledge of cell physiology but also holds promise for advancing medical science and developing innovative therapies.
