Matched pair antibody available for Kanamycin [HRP]: Kanamycin antibody (Catalog # HMABPY044)
Format
Concentrate
Preservative
None
Storage
2-8°C short term, -20°C long term
Introduction
Kanamycin (also known as kanamycin A) is an aminoglycoside bacteriocidal antibiotic, available in oral, intravenous, and intramuscular forms, and used to treat a wide variety of infections. Kanamycin is isolated from the bacterium Streptomyces kanamyceticus and its most commonly used form is kanamycin sulfate.
Antigen Description
Aminoglycosides are a family of bacterial antibiotics that are used in the treatment of specific bacterial infections. They display a concentration dependent killing action and are active against a wide range of aerobic Gram-negative bacilli. Aminoglycosides are molecules that are comprised of an amino group and a sugar group. They operate by inhibiting the bacteria from producing proteins vital to its growth. More specifically, they bind to the bacterial 30S ribosomal subunit where they prevent the translocation of the peptidyl-tRNA from the A-site to the P-site, subsequently giving rise to a misreading of mRNA resulting in the inhibition of protein synthesis. This consequently results in a disruption to the integrity of the bacterial cell membrane. In addition to their use to prevent bacterial infection, aminoglycosides have been used as growth promoters in food producing animals.
Keywords
Kanamycin
Citations
Publication ()
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Background
Kanamycin is an aminoglycoside antibiotic produced by Streptomyces kanamyceticus. It is commonly used in veterinary medicine to treat mastitis, bacillary diarrhea, and pneumonia. This antibiotic is classified as broad-spectrum because it can inhibit the growth of various bacteria, including Escherichia coli, Klebsiella spp., Pseudomonas aeruginosa, and Proteus spp. Kanamycin works by binding to the 30S subunit of ribosomal RNA in Gram-negative bacteria, which disrupts protein synthesis. This binding causes the genetic code to be misread and inhibits translation. Kanamycin consists of three isomers: kanamycin A, B, and C. These isomers have different levels of toxicity. When commercially available, the kanamycin mixture must contain a minimum of 75% kanamycin A and no more than 5% kanamycin B to ensure safety. Horseradish peroxidase (HRP) is a heme-containing enzyme derived from the roots of the horseradish plant (Armoracia rusticana). HRP is widely used as a reporter enzyme in various bioassays and immunoassays due to its exceptional catalytic activity, stability, and sensitivity. It catalyzes the oxidation of a wide range of substrates in the presence of hydrogen peroxide, leading to the generation of a detectable signal, usually a colored or luminescent product.
Figure 1. ELISA detection scheme using the enzyme horseradish peroxidase (HRP). (Source: Spindel, S. et al., 2014)
The conjugation of kanamycin with HRP combines the antimicrobial properties of kanamycin with the signal amplification capabilities of HRP. This conjugate is particularly useful in applications such as enzyme-linked immunosorbent assays (ELISAs), immunohistochemistry (IHC), and Western blotting. In ELISAs, Kanamycin [HRP] can be used to detect the presence of specific antigens or antibodies. In immunohistochemistry and Western blotting, Kanamycin [HRP] conjugate can be used as a detection reagent to visualize the presence of specific proteins. The conjugate binds to specific antibodies that recognize the target protein, and the subsequent addition of a substrate for HRP generates a signal that can be visualized using various detection methods, such as chemiluminescence or colorimetry.
Alternative Names
Kanamycin-HRP Kanamycin, HRP conjugate kanamycin A [HRP] kanamycin A-HRP Kanamycin A, HRP conjugate kana [HRP] kana-HRP Kana, HRP conjugate
References
1. Spindel S, Sapsford K E. Evaluation of optical detection platforms for multiplexed detection of proteins and the need for point-of-care biosensors for clinical use. Sensors. 2014, 14(12): 22313-22341.
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References
Development of immunoassays for the detection of kanamycin in veterinary fields
Monoclonal antibody against kanamycin was prepared, and competitive direct ELISA and immunochromatographic assay were developed using the antibody to detect kanamycin in animal plasma and milk. The monoclonal antibody produced was identified to be IgG1, which has a kappa light chain. No cross-reactivity of the antibody was detected with other aminoglycosides, indicating that the monoclonal antibody was highly specific for kanamycin. Based on competitive direct ELISA, the detection limits of kanamycin were determined to be 1.1 ng/ml in PBS, 1.4 ng/ml in plasma, and 1.0 ng/ml in milk. The concentration of intramuscularly injected kanamycin was successfully monitored in rabbit plasma with competitive direct ELISA. Based on the colloidal gold-based immunochromatographic assay, the detection limits of kanamycin were estimated to be about 6-8 ng/ml in PBS, plasma, and milk. The immunochromatographic assay would be suitable for rapid and simple screening of kanamycin residues in veterinary medicine. Screened positives can be confirmed using a more sensitive laboratory method such as competitive direct ELISA. Therefore, the assays developed in this study could be used to complement each other as well as other laboratory findings. Moreover, instead of slaughtering the animals to obtain test samples, these methods could be applied to determine kanamycin concentration in the plasma of live animals.
Highly sensitive voltammetric determination of kanamycin based on aptamer sensor for signal amplification
In this paper, a novel aptamer sensor for kanamycin was prepared by using a complementary DNA (cDNA) strand of kanamycin aptamer as sensor and horseradish peroxidase (HRP) as a biocatalyst for signal amplification. Gold nanoparticles (AuNPs) and HRP–AuNP–cDNA conjugates were prepared. Transmission electron microscope (TEM) images and ultraviolet-visible absorption spectra were used to characterize the AuNPs. After the cDNA in the conjugates hybridized with kanamycin aptamers immobilized on a gold electrode though Au–thiol interactions, hydroquinone (HQ) and H2O2 in solution were catalyzed by HRP to generate a voltammetric peak current signal. In the presence of kanamycin, aptamers bind with kanamycin to produce a complex on the surface of the gold electrode. The HRP–AuNP–cDNA conjugates therefore fall off from the electrode surface, and the voltammetric signal decreases. The aptamer sensor was successfully applied to determine kanamycin by differential pulse voltammetry (DPV). Under the optimal conditions, the cathodic peak current highly and linearly increased with kanamycin concentrations over the range of 0.010 to 150 μg L-1, with a detection limit of 0.005 μg L-1. This aptamer sensor was applied in the determination of kanamycin in milk with high specificity, sensitivity and selectivity.
COA
Publication 
Figure 1. ELISA detection scheme using the enzyme horseradish peroxidase (HRP).
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