Analytical Data
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Gene name
scaIM
- Application
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Alternative Names
scaIM；Methyltransferase
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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
O52692
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Expression Region
1-304aa
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AA Sequence
MSGRDFGYVIQSSAALWNRLSTFSQRGKALDTRLADIKKALGKPYYETSDVLLYHGDSLELLKSMPQQIFDLTVTSPPYNIGKEYEGVLSIEEYISWCETWMSRVHRATSAGGAFWLNVGYVPVPNQGKAVPIPYLLWDKSPFYMIQEVVWNYGAGVASRKSFSPRNEKFLWYVRDPLNYYFDLDSVRDPNVKYPNQKKNGKLKCNPLGKNPTDVWQFPKVTSGAKRSSVERTAHPAQFPSAVIERVIKACSPSDGVILDPFLGSGTTSLTARKQGRCSVGIEIREDYLDIAVGRLEAEAQSLF
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Molecular Weight
50.2 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
scaIM, or the scorpion toxin-derived antimicrobial peptide, has garnered significant attention in the field of protein engineering and therapeutic development due to its unique structural characteristics and biological activities. Scorpion venom is known to contain a multitude of bioactive compounds, including peptides that exhibit antimicrobial, anti-inflammatory, and cytotoxic properties. Research surrounding scaIM focuses on its potential as a novel antimicrobial agent, particularly in addressing the rising threat of antibiotic-resistant bacteria. Studies indicate that scaIM possesses a distinct mechanism of action, disrupting bacterial cell membranes, which differentiates it from conventional antibiotics and may help overcome resistance issues. Furthermore, the incorporation of scaIM into drug formulations could enhance the efficacy of existing treatments and contribute to the development of innovative therapeutic strategies. This has led to a growing interest in the structural optimization and functional characterization of scaIM, using techniques such as recombinant DNA technology and peptide synthesis. Understanding the mechanisms by which scaIM targets pathogens may pave the way for new research avenues, ultimately leading to the creation of next-generation antimicrobial drugs that are effective against a broad spectrum of harmful microorganisms. The promising results from initial studies underscore the potential of scaIM as a cornerstone in the ongoing fight against infectious diseases, making it a key focus of current and future biomedical research.
