human ll 37 elisa kit  (Cusabio)

Journal: PLOS One

Article Title: Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides

doi: 10.1371/journal.pone.0334029

Figure Lengend Snippet: (A-C) E. coli without treatment. (D-F) Ib-M1. ( G-I ) Ib-M2. (J-L) Ib-M6. (M-O) E. coli treated with PMB. The alterations are indicated as follows: large bulges or spherical elements (asterisk), bulges in formation (white arrowhead), collapsed cells (yellow arrowhead), pores (white arrow), invaginations and deep wrinkles (yellow arrow), debris of cell membranes (white circles), and unchanged surface cells (black squares). All images are representative of three biological replicates with similar results.

Article Snippet: Collectively, our findings reveal the possible mechanisms of action of Ib-M antibacterial peptides against E. coli ATCC 25922 and provide strong scientific evidence supporting their therapeutic potential for combating bacterial pathogens.

Techniques:

Journal: PLOS One

Article Title: Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides

doi: 10.1371/journal.pone.0334029

Figure Lengend Snippet: (A, F) E. coli without treatment. (B, G) Ib-M1. ( C, H, and I ) Ib-M2. (D, J) Ib-M6. (E, K) E. coli treated with PMB. The alterations are indicated as follows: cytoplasmic retraction (black bracket), bulges (white arrowhead), invagination (yellow arrow), electron-dense material (black arrow and arrowhead), lysed cells (black oval), cytoplasmic vacuoles (thin black arrow), cellular debris-lipid material (black square), and pore (white arrow). All images are representative of three biologically independent assays performed with similar results.

Article Snippet: Collectively, our findings reveal the possible mechanisms of action of Ib-M antibacterial peptides against E. coli ATCC 25922 and provide strong scientific evidence supporting their therapeutic potential for combating bacterial pathogens.

Techniques:

Journal: PLOS One

Article Title: Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides

doi: 10.1371/journal.pone.0334029

Figure Lengend Snippet: Interaction of Ib-M peptides with LPS and permeabilization of the E. coli outer membrane. (A) Determination of BODIPY-TR cadaverine displacement from LPS by Ib-M peptides after 60 min of exposure. PMB was utilized as a positive control. Values are expressed as mean ± SD of three independent assays. Statistical analysis was performed using ANOVA with Tukey’s multiple comparison test. (B) NPN fluorescence measurement upon exposure of E. coli ATCC 25922 to Ib-M1 peptide. PMB was used as the positive control at a concentration of 12.5 µM. The negative control was comprised of bacteria without the addition of peptides. Measurements were obtained at minute 60. The mean ± SD of a representative assay is presented. Significant differences were established and are denoted as *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001; ns indicates no significance.

Article Snippet: Collectively, our findings reveal the possible mechanisms of action of Ib-M antibacterial peptides against E. coli ATCC 25922 and provide strong scientific evidence supporting their therapeutic potential for combating bacterial pathogens.

Techniques: Membrane, Positive Control, Comparison, Fluorescence, Concentration Assay, Negative Control, Bacteria

Journal: PLOS One

Article Title: Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides

doi: 10.1371/journal.pone.0334029

Figure Lengend Snippet: Inner permeabilization of E. coli ML35. ( A ) Ib-M1. ( B ) Ib-M2. ( C ) Ib-M6. Measurements were obtained every five min for 8 h. PBS without the addition of ONPG served as the negative control. ( D ) PMB and ( E ) streptomycin were employed as the positive and negative controls, respectively. Time-dependent cytoplasmic membrane depolarization of E. coli ATCC25922 induced by ( F ) Ib-M1, ( G ) Ib-M2, and ( H ) Ib-M6; as determined using the membrane potential-sensitive fluorescent dye, DiSC 3 . Dye release was monitored by measuring fluorescence at an excitation wavelength of 620 nm and an emission wavelength of 670 nm. Triton X-100 was used as the positive control. Data are expressed as mean ± SD of three independent assays.

Article Snippet: Collectively, our findings reveal the possible mechanisms of action of Ib-M antibacterial peptides against E. coli ATCC 25922 and provide strong scientific evidence supporting their therapeutic potential for combating bacterial pathogens.

Techniques: Negative Control, Membrane, Fluorescence, Positive Control

Journal: Gut microbes

Article Title: Helminth reshapes host gut microbiota and immunoregulation by deploying an antimicrobial program of innate immunity.

doi: 10.1080/19490976.2025.2496447

Figure Lengend Snippet: Figure 2. CRAMP drives the expansion of lactobacilli bacteria during Emu infection. (a) ELISA measurements of antibacterial peptides (AMPs) in serum and colon tissue in the naive mice and mice infected with Emu 6 weeks post-infection. The expression levels were scaled between naive and infection and are shown in Z-score. (b) The protein level of CRAMP in the serum of the mice at the early or chronic infection stage. (c) The increased level of CRAMP in the feces of the mice 2 hours after injection with mCRAMP. (d and e) the abundances of Lactobacillus and Enterobacteriaceae (d) and L/E ratio (e) in the feces of the mice injected with mouse CRAMP or vehicle control. qPCR analyses were performed every two days. (f, g, and h) the abundances of Lactobacillus (f) and Enterobacteriaceae (g) and

Article Snippet: The level of each antibacterial peptide was evaluated using ELISA methods as per the recommendation of each manufacturer, including CRAMP ELISA kit (Cat. CSB-E5061m, Cusabio), Reg3g ELISA kit (Cat. CSB-EL9549MO, Cusabio), Sprr2a ELISA kit (Cat. K8–14835, KIRbio), Lyz1 ELISA kit (Cat. K8–14839), Retnla ELISA kit (Cat. K8–02975), α-defensins ELISA kit (Cat. K6–02404, KIRbio), β-defensins ELISA kit (Cat. K6–02440, KIRbio), Reg3α ELISA kit (Cat. K6–14918, KIRbio), and human LL-37 ELISA kit (Cat. CSBEL4476HU, Cusabio).

Techniques: Bacteria, Infection, Enzyme-linked Immunosorbent Assay, Expressing, Injection, Control

Journal: Microbiology

Article Title: Purification and characterization of a novel antibacterial peptide against Clostridium perfringens

doi: 10.1099/mic.0.001573

Figure Lengend Snippet: Partial purification of an antibacterial peptide from the CFS of B. velezensis HG88. ( a ) FPLC chromatogram showing cation exchange chromatography of the CFS. Fractions 21 and 22 eluted at 0.23 M NaCl, showed antimicrobial activity towards C. perfringens CP1 and had an MBC of ~632.5 µg ml −1 . ( b ) Tris-tricine SDS-PAGE of pooled fractions 21 and 22, showing a band consisting of the protein of interest with the M W of ~9 kDa.

Article Snippet: The aforementioned PB6 strain produced an antibacterial peptide of 960–983 Da in size that inhibited the growth of C. perfringens ATCC 13124 and was resistant to degradation under high temperatures (100 and 121 °C) and to trypsin digestion, due to the presence of lipid or carbohydrate moieties that modified the peptide [ ].

Techniques: Purification, Chromatography, Activity Assay, SDS Page

Journal: Microbiology

Article Title: Purification and characterization of a novel antibacterial peptide against Clostridium perfringens

doi: 10.1099/mic.0.001573

Figure Lengend Snippet: Protein fragment coverage map generated through LC-MS peptide fingerprinting. Results from MS analysis of the in-gel digested antibacterial peptide that is shown in . A protein with a theoretical size of 12.34 kDa was identified through matching 39 peptides with 64% coverage of the HG88_03711 gene.

Article Snippet: The aforementioned PB6 strain produced an antibacterial peptide of 960–983 Da in size that inhibited the growth of C. perfringens ATCC 13124 and was resistant to degradation under high temperatures (100 and 121 °C) and to trypsin digestion, due to the presence of lipid or carbohydrate moieties that modified the peptide [ ].

Techniques: Generated, Liquid Chromatography with Mass Spectroscopy