Analytical Data
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Gene name
PMAP23
- Application
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Alternative Names
Myeloid antibacterial peptide 23
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Species
Pig
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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
P49930
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Expression Region
131-153aa
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Molecular Weight
19.0 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
PMAP23, or Porcine Multivalent Antimicrobial Peptide 23, is a promising candidate in the field of antimicrobial research, particularly due to its potential in addressing the rising concern of antibiotic resistance. Derived from pigs, PMAP23 exhibits a broad-spectrum antimicrobial activity against various pathogens, including both Gram-positive and Gram-negative bacteria, as well as fungi. The increasing incidences of multi-drug resistant infections necessitate the exploration of novel antimicrobial agents, and peptides like PMAP23 have emerged as vital alternatives due to their unique mechanisms of action, which often involve disruption of microbial membranes. In recent years, recombinant techniques have enabled the efficient production of PMAP23, facilitating comprehensive studies on its structure-function relationships and biological efficacy. Researchers are focused on evaluating its potential applications in both veterinary and human medicine, aiming to optimize its therapeutic properties through modifications that enhance its stability and reduce toxicity. Additionally, PMAP23's ability to synergize with other antimicrobial agents further enhances its appeal in combination therapies designed to combat resistant strains. Overall, the investigation of PMAP23 and similar peptides holds significant promise for the development of innovative and effective antimicrobial strategies in an era marked by increasing resistance challenges.
