Analytical Data
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Gene name
Pandinin
- Application
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Alternative Names
Non-disulfide-bridged peptide 3.1 Short name: NDBP-3.1 Non-disulfide-bridged peptide 4.1 Short name: NDBP-4.1
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Species
Pandinus imperator
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Source
Yeast
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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
P83240
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Expression Region
1-24aa
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Molecular Weight
4.6 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
Pandinin is a novel recombinant protein derived from the venom of the Brazilian spider, Phoneutria nigriventer, known for its potent neurotoxic properties. Research on Pandinin has emerged due to the growing interest in spider venoms as potential sources of new therapeutic agents. The unique structure and biochemical characteristics of Pandinin make it a promising candidate for drug development, particularly in the field of pain management and neurological disorders. Initial studies have indicated that Pandinin has a high affinity for specific ion channels, which may contribute to its therapeutic effects. Furthermore, as the demand for alternative pain relief methods rises, Pandinin's ability to modulate pain sensation without the common side effects associated with traditional analgesics presents an exciting avenue for exploration. Researchers are actively investigating the molecular mechanisms underlying its action, optimizing its production through recombinant DNA technology, and evaluating its efficacy in preclinical models. The ultimate goal is to harness Pandinin's potential to develop safer and more effective treatments, addressing the critical need for innovative solutions in pain therapy and neuropharmacology.
