biotinylated polyclonal rabbit anti-human cxcl8 antibodies (PeproTech)
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biotinylated polyclonal rabbit anti-human cxcl8 antibodies
Biotinylated Polyclonal Rabbit Anti Human Cxcl8 Antibodies, supplied by PeproTech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/biotinylated+polyclonal+rabbit+anti-human+cxcl8/recombinant+human+il+2/pm39625496-88-25-32
Average 90 stars, based on 1 article reviews
Biotinylated Polyclonal Rabbit Anti Human Cxcl8 Antibodies, supplied by PeproTech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/biotinylated+polyclonal+rabbit+anti-human+cxcl8/recombinant+human+il+2/pm39625496-88-25-32
Average 90 stars, based on 1 article reviews
biotinylated polyclonal rabbit anti-human cxcl8 antibodies - by Bioz Stars,
2026-10
90/100 stars
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Labeling:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Synthesized:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Purification:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Software:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Binding Assay:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Fluorescence:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Comparison:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Concentration Assay:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with MANN-WHITNEY:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Flow Cytometry:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Inhibition:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Migration:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Injection:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Staining:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Saline:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Activity Assay:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Blocking Assay:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Activation Assay:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Transfection:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Incubation:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Mass Spectrometry:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Generated:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Control:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with Modification:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with In Vivo:Article Title: CXCL9-Derived Peptides Differentially Inhibit Neutrophil Migration In Vivo through Interference with Glycosaminoglycan Interactions Article Snippet: Subsequently, bound CXCL8 or CXCL1 was detected with biotinylated polyclonal rabbit anti-human CXCL8 or Article Title: Biological Activity of CXCL8 Forms Generated by Alternative Cleavage of the Signal Peptide or by Aminopeptidase-Mediated Truncation Article Snippet: Unbound CXCL8 was removed by three washes with SAB and bound CXCL8 was detected with |
![Proteolytic processing of intact CXCL8 in BAL fluid. ( A ) Recombinant human CXCL8(1–77) [125 ng] was spiked in 10 µL of BAL fluid supernatant from CLAD ( n = 12), infected ( n = 6) or stable LTx patients ( n = 6) and from patients with COVID-19 ( n = 10) or influenza ( n = 7). After incubation for 3 h at 37 °C, CXCL8 proteolysis was analyzed by ISTAMPA. ( B ) CXCL8 proteoforms were also determined immediately after spiking CXCL8 [without 37 °C incubation but including the required 30 min pre-purification of the CXCL8 proteoforms at room temperature (RT) as part of the ISTAMPA procedure] and after 16 h of incubation at 37 °C in the COVID-19 BAL fluids. CXCL8 proteoforms were presented according to their relative abundance in the BAL fluids, expressed as percentage of total CXCL8. ( C , D ) Correlation between the relative abundance of the intact CXCL8(1–77) or the truncated CXCL8(6–77) proteoform after 3 h incubation at 37 °C and the elastinolytic activity in the COVID-19 BAL fluid samples . Data are shown as box-and-whisker plots (box: median with interquartile range, whiskers: full data distribution), with each dot representing an individual BAL fluid sample, and statistically analyzed by Kruskal-Wallis tests with Dunn’s multiple comparisons tests: * p < 0.05; **** p < 0.0001. Correlation analysis was performed calculating a Spearman correlation coefficient and plotted utilizing a simple linear regression line](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_5237/pmc11615237/pmc11615237__18_2024_5500_Fig6_HTML.jpg)
![Inhibition of proteolytic processing of CXCL8 in BAL fluid. ( A ) Recombinant human CXCL8(6–77) [125 ng] was spiked in 10 µL of BAL fluid supernatant ( n = 3–6) from COVID-19 (indicated by dots) and CLAD patients (indicated by triangles) and incubated for 3 h at 37 °C, in the absence or presence of the metalloprotease inhibitor EDTA. ( B ) Recombinant human CXCL8(1–77) [125 ng] was spiked in 10 µL of BAL fluid supernatant ( n = 8–9) from COVID-19 (dots) and CLAD patients (triangles) and incubated for 3 h at 37 °C, in the absence or presence of the serine protease inhibitor AEBSF or/and the metalloprotease inhibitor EDTA. After incubation, CXCL8 proteolysis was determined by ISTAMPA. All CXCL8 proteoforms were presented according to their relative abundance in the sample, expressed as percentage of total CXCL8. Data are shown as box-and-whisker plots (box: median with interquartile range, whiskers: full data distribution), with each dot representing an individual BAL fluid sample, and statistically analyzed by Mann-Whitney U tests or Kruskal-Wallis tests with Dunn’s multiple comparisons tests: * p < 0.05; *** p < 0.001; **** p < 0.0001](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_5237/pmc11615237/pmc11615237__18_2024_5500_Fig7_HTML.jpg)
![Detection of CXCL8 proteoforms by top-down tandem mass spectrometry. (A) Parameters are optimized to ensure that only the acid-labile Asp-Pro (DP) bond breaks during low-energy fragmentation and only two fragment ions are generated. (B) Mass spectra (single MS) showing the intensity of multiple charged ions of CXCL8(1-77), CXCL8(6-77) and CXCL8(9-77) as a function of their m/z values. Ions with m/z values of 892.8 [for CXCL8(1-77)], 932.3 [for CXCL8(6-77)] or 900.4 [for CXCL8(9-77)] were isolated and fragmented with low energy CID. The resulting fragmentation spectra are shown in the lower panels in (C) . Diamonds indicate the m/z value of the precursor ions selected for fragmentation. Extracted ion chromatograms (EIC) (top panels) show the detection of m/z values (±0.5) of the two signature fragment ions during protein elution. Relative quantification of CXCL8 forms is performed based on the intensity of the two major fragment ions in the EIC. (D) Dose-response curves for the simultaneous quantification of three CXCL8 forms in MRM mode (amounts ranging from 3.1 pg to 12.5 ng). Regression analysis was performed to fit curves to data. Results are represented as mean ± SEM ( n ≥ 4).](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_1300/pmc07991300/pmc07991300__fimmu-12-644725-g0002.jpg)
![CXCL9(74-93) interacts with cellular glycosaminoglycans (GAGs) . The interaction of the COOH-terminal CXCL9 peptides with Chinese hamster ovary (CHO) cells was assessed by flow cytometric analysis. (A) CHO cells were treated with dilutions of NH 2 -terminally biotinylated CXCL9(74-103) and CXCL9(74-93), which were detected by streptavidin-allophycocyanin. (B) To ensure that the binding of CXCL9(74-93) was GAG-mediated, CHO cells were treated with sodium chlorate (NaClO 3 ) to reduce the sulfation of GAGs. Binding of biotinylated CXCL9(74-93) to cells, treated or untreated with NaClO 3 , was detected by streptavidin-allophycocyanin. The mean (+SEM) fluorescence intensity of bound biotinylated CXCL9 peptides to CHO cells is indicated on the y -axis ( n ≥ 4). A statistical comparison to evaluate the binding of biotinylated peptides on CHO cells [compared to the corresponding concentration of CXCL9(74-103) (A) or to the binding to cells not treated with NaClO 3 (B) ] was performed using the Mann–Whitney U -test (* p < 0.05; * * p < 0.01).](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_3902/pmc05423902/pmc05423902__fimmu-08-00530-g002.jpg)
![CXCL9(74-93) competes with CXCL8 for binding to heparin, heparan sulfate (HS), and cellular glycosaminoglycans (GAGs) . Competition between CXCL8 and COOH-terminal CXCL9 or CXCL4 peptides for binding to immobilized heparin (A) or HS (B) and to Chinese hamster ovary (CHO) cells (C) was performed. (A) and (B) CXCL8(1-77) (0–300 nM) was added to heparin-coated or HS-coated 96-well plates in the presence or absence of the indicated excess of COOH-terminal peptide [CXCL9(74-103) (■), CXCL9(74-93) (□), CXCL9(86-103) (Δ), CXCL4(47-70) (▴)]. Bound CXCL8 was detected with biotinylated anti-human CXCL8 antibodies. (C) Binding of NH 2 -terminally biotinylated CXCL8(1-77) (300 nM) to CHO cells in the presence or absence of an excess CXCL9 peptide was detected by streptavidin-allophycocyanin and flow cytometry. The mean (± SEM) percentage inhibition of binding of CXCL8(1-77) to heparin, HS or cellular GAGs is indicated on the y -axis ( n ≥ 4). Statistical comparison of the different competitors with CXCL9(74–103) was performed using the Mann–Whitney U- test (* p < 0.05).](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_3902/pmc05423902/pmc05423902__fimmu-08-00530-g003.jpg)
![CXCL9(74-93) is a less potent competitor for CXCL1 binding to glycosaminoglycans (GAGs) . Competition between CXCL1 and COOH-terminal CXCL9 peptides for binding to immobilized heparan sulfate (HS) (A) and chondroitin sulfate (CS) (B) was performed. Dilutions of CXCL1 were added to GAGs in 96-well plates in the presence or absence of the indicated excess of COOH-terminal peptide [CXCL9(74-103) (■), CXCL9(74-93) (□), CXCL9(86-103) (Δ)]. Bound CXCL1 was detected with biotinylated polyclonal goat anti-mouse CXCL1 antibodies. The mean (± SEM) percentage inhibition of CXCL1 binding to GAGs is indicated on the y- axis ( n ≥ 3). Statistical comparison of the different competitors with CXCL9(74–103) was performed using the Mann–Whitney U- test.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_3902/pmc05423902/pmc05423902__fimmu-08-00530-g006.jpg)
