Analytical Data
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Gene name
def
- Application
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Alternative Names
Polypeptide deformylase
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Species
Escherichia coli O157:H7
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0A6K5
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Expression Region
2-169aa
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Molecular Weight
35.2 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
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Protein Description
Defensins are a family of small, cationic peptides that play a crucial role in the innate immune response across a wide range of organisms, including plants, insects, and mammals. These proteins are known for their antimicrobial properties, providing a first line of defense against pathogens such as bacteria, fungi, and viruses. Research into defensins has gained prominence due to their potential therapeutic applications, especially in the context of rising antibiotic resistance. Additionally, defensins exhibit various biological activities, including immunomodulation and wound healing, making them attractive candidates for drug development. The study of defensin recombinants is particularly important as it allows researchers to explore structure-function relationships, enhance peptide stability and activity, and produce these molecules at a larger scale for clinical and agricultural applications. By employing recombinant DNA technology, scientists can express and purify defensins in heterologous systems, facilitating detailed biochemical studies and the design of novel therapeutics. Overall, the investigation of defensin recombinants has significant implications for enhancing our understanding of host defense mechanisms and developing innovative solutions to combat infectious diseases.
