Analytical Data
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Gene name
alphaIC
- Application
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Alternative Names
Dermonecrotic toxin LamSicTox-alphaIC1; EC 4.6.1.-; Phospholipase D; PLD; Sphingomyelin phosphodiesterase D; SMD; SMase D; Sphingomyelinase D; Fragment
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Species
Loxosceles amazonica
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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
C0JAZ9
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Expression Region
1-273aa
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Molecular Weight
34.8 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
AlphaIC recombinant proteins are an important focus of research due to their potential applications in various fields such as medicine, biotechnology, and agriculture. The AlphaIC family consists of proteins that play crucial roles in cellular processes, including signal transduction, cell growth, and immune response. The study of these proteins has gained traction as scientists seek to understand their structure-function relationships and the mechanisms underlying their biological activities. Advances in recombinant DNA technology have made it feasible to produce AlphaIC proteins in vitro, allowing for the detailed characterization of their functions and interactions. This research is particularly relevant in therapeutic contexts, where AlphaIC proteins may be leveraged for drug development, including targeted therapies for diseases such as cancer and autoimmune disorders. Furthermore, understanding the properties of these proteins can lead to innovations in crop improvement and pest resistance. As a result, the investigation of AlphaIC recombinant proteins is not only fundamental for basic biological research but also has significant implications for developing novel health and agricultural solutions.
