Analytical Data
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Gene name
CTXI
- Application
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Alternative Names
CTXI；
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Species
E.coli
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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
P15220
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Expression Region
1-36aa
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AA Sequence
MCMPCFTTRPDMAQQCRACCKGRGKCFGPQCLCGYD
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Molecular Weight
4.0 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
CTXI (Crotalus toxicogenin I) is a recombinant protein derived from the venom of the Eastern diamondback rattlesnake (Crotalus adamanteus), known for its complex array of biologically active components. The research background of CTXI focuses on its potential applications in therapeutic and biotechnological fields, given its unique properties and mechanisms of action. The increasing interest in snake venoms as a source of novel biomolecules has prompted scientists to investigate CTXI for its ability to modulate various biological pathways, including anti-inflammatory and analgesic effects. Moreover, the recombinant production of CTXI offers advantages over traditional extraction methods from snakes, such as sustainability and scalability, which are crucial for meeting growing demand in medical research. Understanding the structure-function relationship of CTXI can lead to the development of new drugs, particularly in pain management and autoimmune diseases. Additionally, the study of CTXI sheds light on venom evolution and offers insights into the ecological roles of snake venoms in nature. As such, ongoing research into CTXI not only aims to harness its therapeutic potential but also contributes to broader scientific knowledge in toxinology and molecular biology.
