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Strep-avidin conjugated horseradish peroxidase

Strep-avidin conjugated horseradish peroxidase is a powerful tool for a variety of biological assays and experiments.
This enzyme conjugate combines the high-affinity binding of streptavidin and avidin with the versatile catalytic properties of horseradish peroxidase, enabling sensitive detection and amplification of target analytes.
Researchers can optimize their protocols and experimental conditions using PubCompare.ai, an AI-driven platform that helps locate the best procedures from literature, preprints, and patents.
This intelligent comparison tool empowers reproducible and accruate research by discovering the optimal products and parameters for your next experiment.

Most cited protocols related to «Strep-avidin conjugated horseradish peroxidase»

1
Furin Expression in Lung and Breast Cancers
Cited 9 times
Immunohistochemistry (IHC) was performed in Chinese lung and breast cancer tissues using the furin antibody 31 , 32 (link), 34 (link). Briefly, the de-paraffinized and re-hydrated tissue sections were treated in the 10 μM sodium citrate buffer at 95 °C for 12 minutes for antigen retrieval. The treated tissue slides were further incubated in the solution with 3% H2O2 for quenching the endogenous peroxidase. After blocking with 5% bovine serum albumin (BSA), the tissue slides were incubated with the primary antibody by overnight at 4 °C (rabbit monoclonal antibodies, 1:200; cat #: ab183495, Cambridge, CB2 0AX, UK) and then the biotin-conjugated secondary antibody (cat #: SP-9000, ZSGB-Bio, CN) for 60 minutes at room temperature. The bound secondary antibody was visualized by sequentially incubating with the Streptavidin-conjugated horseradish peroxidase (HRP) and its substrate diaminobenzidine (ZLI-9017, ZSGB-Bio, CN).
Cordycepin (CD) was purchased from Chengdu Must Bio-Technology Co.Ltd (Chengdu, Sichuan, P. R. China). Western blotting analysis for furin expression was performed in lung cancer cell line H1975 and breast cancer cell line BT549 with CD treatments (0, 10 µm, 20 µm, 40 µm) for 24 hours. The furin antibody for western blotting was used as same as IHC (rabbit monoclonal antibodies, cat #: ab183495, Cambridge, CB2 0AX, UK). The semi-quantitative RT-PCR for furin expression was performed in breast cancer cell line BT549 with CD treatments (0, 10 µm, 20 µm, 40 µm) for 24 hours. RT-PCR primers for furin were as follows, 5'-tgtggtgtaggtgtggccta-3' (RT-furin-L), 5'-gctgatggacagcgtgtaga-3' (RT-furin-R). GAPDH was served as internal control. All experiments were repeated at three times.
Li D., Liu X., Zhang L., He J., Chen X., Liu S., Fu J., Fu S., Chen H., Fu J, & Cheng J. (2021). COVID-19 disease and malignant cancers: The impact for the furin gene expression in susceptibility to SARS-CoV-2. International Journal of Biological Sciences, 17(14), 3954-3967.
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Publication 2021
Antigens Biotin Buffers Cell Lines Chinese cordycepin FURIN protein, human GAPDH protein, human Immunoglobulins Immunohistochemistry Lung Lung Cancer Malignant Neoplasm of Breast MCF-7 Cells Monoclonal Antibodies Oligonucleotide Primers Peroxidase Peroxide, Hydrogen Rabbits Reverse Transcriptase Polymerase Chain Reaction Serum Albumin, Bovine Sodium Citrate Strep-avidin conjugated horseradish peroxidase Tissues Western Blot
2
Quantitative Binding Assay for IGFBP-3 and CD44
Cited 7 times
Most of the material used was purchased as we previously reported [48, 60, 66]. Phosphate‐buffered saline (PBS), streptavidin‐conjugated horseradish peroxidase (HRP), phenylmethylsulfonyl fluoride (PMSF), TCEP‐HCl, N‐ethylmaleimide, and HA‐biotin (B1557) were purchased from Sigma‐Aldrich (Burlington, MA, USA). PNGase F was from New England Biolabs (Ipswich, MA, USA). Recombinant human IGFBP‐3 protein (YCP1009, UniProt accession ID: P17936) was purchased from Speed BioSystems (Gaithersburg, MD, USA). Human recombinant CD44 protein (12211‐H08H) was purchased from Sino Biological (Wayne, PA, USA). Nonglycosylated recombinant IGFBP‐3 (MBS142177) was from MyBioSource (San Diego, CA, USA). HN (018‐26) and biotin‐HN (B‐018‐26, UniProt accession ID: Q8IVG9) were purchased from Phoenix Pharmaceuticals (Burlingame, CA, USA). CD44 antibody (5F12) (MA5‐12394), mouse IgG isotype control (mIgG), ultra 3,3′,5,5′‐tetramethylbenzidine (TMB)‐ELISA substrate solution, Halt Protease and Phosphatase Inhibitor Cocktail, and Nunc MaxiSorpTM 96‐well flat‐bottom plates were from Thermo Fisher. The SuperSignal West Pico Luminol (Chemiluminescence) Reagent and BCA Protein Assay Kit were from Pierce (Dallas, TX, USA).
Dorandish S., Devos J., Clegg B., Price D., Muterspaugh R., Guthrie J., Heyl D.L, & Evans H.G. (2020). Biochemical determinants of the IGFBP‐3–hyaluronan interaction. FEBS Open Bio, 10(8), 1668-1684.
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Publication 2020
3,3',5,5'-tetramethylbenzidine Biological Assay Biopharmaceuticals Biotin CD44 protein, human Chemiluminescence CXCL9 protein, human Enzyme-Linked Immunosorbent Assay Ethylmaleimide Glycopeptidase F Immunoglobulin Isotypes Immunoglobulins Insulin-Like Growth Factor Binding Protein 3 isononanoyl oxybenzene sulfonate Luminol Mus Peptide Hydrolases Pharmaceutical Preparations Phenylmethylsulfonyl Fluoride Phosphates Phosphoric Monoester Hydrolases Proteins Saline Solution Strep-avidin conjugated horseradish peroxidase tris(2-carboxyethyl)phosphine
3
Immunohistochemical Analysis of Formalin-Fixed, Paraffin-Embedded Tissue
Cited 5 times
The tumors of the mice were fixed in formalin and embedded in paraffin. The 2-μm-thick consecutive sections were cut from the paraffin-embedded tissue blocks and floated onto glass slides. The slides were first incubated at 65 °C for 1 h and then deparaffinized in xylene, rehydrated in graded ethanol solutions, and boiled in Trilogy reagent (Cell Marque, Rocklin, CA, USA) for 10 min for antigen retrieval. After washing with 1 × PBS, the slides were immersed in 3% hydrogen peroxide for 10 min to suppress endogenous peroxidase activity. After triple-rinsing with 1 × PBS, the sections were exposed to the appropriate primary antibodies for 1 h at room temperature, after which they were rinsed three times with 1 × PBS and incubated with a biotinylated secondary antibody (Dako, Glostrup, Denmark) for 25 min. After three rinses with 1 × PBS, the slides were treated with horseradish peroxidase-conjugated streptavidin for 25 min. The peroxidase activity was developed with DAB (Dako), followed by counterstaining with hematoxylin.
Chen C.C., Chen C.Y., Ueng S.H., Hsueh C., Yeh C.T., Ho J.Y., Chou L.F, & Wang T.H. (2018). Corylin increases the sensitivity of hepatocellular carcinoma cells to chemotherapy through long noncoding RNA RAD51-AS1-mediated inhibition of DNA repair. Cell Death & Disease, 9(5), 543.
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Publication 2018
Antibodies Antigens Cells Ethanol Formalin Hematoxylin Immunoglobulins Mus Neoplasms Paraffin Embedding Peroxidase Peroxide, Hydrogen Strep-avidin conjugated horseradish peroxidase Tissues Xylene
4
Quantifying Eosinophil-Derived Proteins in Samples
Cited 5 times
ESGP and CLC/Gal-10 levels present in EST samples and biopsy extracts were determined using commercial (EDN, ECP; MBL International, Woburn, MA, USA) or inhouse developed (MBP1, CLC/Gal-10, EPX) ELISAs. Assays for EDN and ECP were performed according to the manufacturer's instructions. Double-antibody sandwich ELISAs for MBP1 and CLC/Gal-10 were developed and standardised at the Ackerman laboratory (Chicago, IL, USA) and for EPX at the Lee laboratory (Scottsdale, AZ, USA). MBP1 and CLC/Gal-10 ELISAs used standard curves generated using the purified eosinophil-derived protein, prepared as previously described.7 (link)
20–22 For MBP1, mouse monoclonal antibodies were used for both capture and detection (mouse anti-human MBP1-clones, J14-8A2 and J13-6B6, respectively, kindly provided by Dr Hirohito Kita, Mayo Clinic, Rochester, Minnesota, USA), the detection antibody being biotinylated and detected using streptavidin-conjugated horseradish peroxidase (ExtraAvidin Peroxidase, E2886; Sigma-Aldrich, St. Louis, Missouri, USA) and FAST OPD Tablet substrate (P9187; Sigma-Aldrich). CLC/Gal-10 ELISAs used a mouse monoclonal capture antibody (Anti-human Gal-10/CLC, Cell Sciences, Canton, Massachusetts, USA), whereas the detection antibody was a CLC/Gal-10 affinity purified rabbit polyclonal antibody prepared as previously described.7 (link) Detection antibodies for the MBP1 and CLC/Gal-10 ELISAs were biotinylated using a Biotin-XX Microscale Protein Labelling Kit (B30010; Molecular Probes, Invitrogen, Eugene, Oregon, USA) according to the manufacturer's instructions. MBP1 and CLC/Gal-10 ELISA assays detected these eosinophil-derived proteins in the ranges of 11.8–750 and 0.125–16 ng/ml, respectively, with recoveries of 80%–100% and 100%–120%, signal to noise ratios >5 and coefficient of variation (CV) of 15%.
Specific parameters and detailed protocol and methods associated with the EPX-based ELISA in mice have been recently described.23 (link) EPX ELISA detected EPX in the range of 8–1024 ng/ml, with recovery of 90%, signal to noise ratios >15 and an assay CV of 13%.
Furuta G.T., Kagalwalla A.F., Lee J.J., Alumkal P., Maybruck B.T., Fillon S., Masterson J.C., Ochkur S., Protheroe C., Moore W., Pan Z., Amsden K., Robinson Z., Capocelli K., Mukkada V., Atkins D., Fleischer D., Hosford L., Kwatia M.A., Schroeder S., Kelly C., Lovell M., Melin-Aldana H, & Ackerman S.J. (2012). The oesophageal string test: a novel, minimally invasive method measures mucosal inflammation in eosinophilic oesophagitis. Gut, 62(10), 1395-1405.
Publication 2012
Antibodies Biological Assay Biopsy Biotin Cells CLC protein, human Enzyme-Linked Immunosorbent Assay Eosinophil Homo sapiens Immunoglobulins MBL2 protein, human ML 1024 Molecular Probes Monoclonal Antibodies Mus Peroxidase Proteins Rabbits Strep-avidin conjugated horseradish peroxidase Tablet
5
Exosomal PD-L1 Binding to PD-1 Assay
Cited 4 times
To test the binding of exosomal PD-L1 to PD-1, 100 μl of exosome samples of different concentrations were captured onto PD-L1 antibody (clone 5H1-A3)-coated 96-well ELISA plates by overnight incubation at 4°C. Then 100 μl of 4 μg/ml biotin-labeled human PD-1 protein (BPS Bioscience, Cat# 71109) was added and incubated for 2 hr at room temperature. A total of 100 μl per well of horseradish peroxidase-conjugated streptavidin (BD Biosciences) diluted in PBS containing 0.1% BSA was then added and incubated for 1 hr at room temperature. Plates were developed with tetramethylbenzidine (Pierce) and stopped using 0.5N H2SO4. The plates were read at 450 nm with a BioTek plate reader. Recombinant human PD-L1 protein directly coated onto the plates was used as the positive control. Biotin-labeled mouse CD8 protein instead of biotin-labeled human PD-1 protein was used as the negative control.
Chen G., Huang A.C., Zhang W., Zhang G., Wu M., Xu W., Yu Z., Yang J., Wang B., Sun H., Xia H., Man Q., Zhong W., Antelo L.F., Wu B., Xiong X., Liu X., Guan L., Li T., Liu S., Yang R., Lu Y., Dong L., McGettigan S., Somasundaram R., Radhakrishnan R., Mills G., Lu Y., Kim J., Chen Y.H., Dong H., Zhao Y., Karakousis G.C., Gangadhar T.C., Schuchter L.M., Herlyn M., Wherry E.J., Xu X, & Guo W. (2018). Exosomal PD-L1 Contributes to Immunosuppression and is Associated with anti-PD-1 Response. Nature, 560(7718), 382-386.
Publication 2018
3,3',5,5'-tetramethylbenzidine Biological Assay Biotin CD274 protein, human Clone Cells Enzyme-Linked Immunosorbent Assay Exosomes Homo sapiens Immunoglobulins Mus PDCD1 protein, human Pdcd1 protein, mouse Strep-avidin conjugated horseradish peroxidase

Most recents protocols related to «Strep-avidin conjugated horseradish peroxidase»

1
Immunohistochemical Analysis of Microglia and Astrocytes
Mice were anesthetized, perfused and sacrificed. Brains were then removed, fixed in 4% paraformaldehyde for 48 h, and dehydrated with gradient sucrose in phosphate buffered saline (PBS). The brains were embedded in optimal cutting temperature compound (OCT) and sectioned on a freezing microtome (CM3050S, Leica, Wetzlar, Germany). The coronal sections (40 μm in thickness) were incubated overnight with anti-goat Iba1 antibody (1:400, 019-19741, Wako, Richmond, VA, United States) and anti-mouse Gfap antibody (1:400; MAB360, Millipore, Darmstadt, Germany).
For immunohistochemical staining, the slices were incubated with biotinylated immunoglobulin G (IgG), followed by streptavidin-conjugated horseradish peroxidase (VECTASTAIN ABC Kit, Zhongshan Jinqiao, Beijing, China), and finally was visualized by reacting with hydrogen peroxide (DAB Kit, Zhongshan Jinqiao). Images were captured using a Leica SCN400 scanner.
For immunofluorescent staining, the sections were labeled with TRITC AffiniPure goat anti-rabbit IgG (111-025-003, Jackson ImmunoResearch) fluorescent secondary antibody, and the images were acquired by Nikon confocal microscope (Nikon, Melville, NY, United Stats). For activated microglia quantification, we determined the activated microglia by larger soma area, shorter and bolder processes.
Li X., Peng Z., Jiang L., Zhang P., Yang P., Yuan Z, & Cheng J. (2023). Dlg1 deletion in microglia ameliorates chronic restraint stress induced mice depression-like behavior. Frontiers in Pharmacology, 14, 1124845.
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Publication 2023
anti-GFAP autoantibodies Antibodies, Anti-Idiotypic Brain Carisoprodol Fluorescent Antibody Technique Goat Immunoglobulin G Mice, House Microglia Microscopy, Confocal Microtomy paraform Peroxide, Hydrogen Phosphates Rabbits Saline Solution Strep-avidin conjugated horseradish peroxidase Sucrose tetramethylrhodamine isothiocyanate
2
Influenza Antibody Detection ELISA
Blood samples were taken by puncture of the saphenous vein. Serum was obtained by centrifugation at 17,000 × g for 10 min, and then the supernatant was transferred to a new microcentrifuge tube and centrifuged again at 17,000 × g for 5 min. Sera were stored at −20°C.
For ELISA, 96-well microtiter plates (Costar 3590, Corning, NY, USA) were coated with one of the following recombinant influenza HA proteins: A/Puerto Rico/8/1934(H1N1) (cat. no. 11684-V08H, Sino Biological), A/Viet Nam/1194/2004(H5N1) (cat. no. 11062-V08H1, Sino Biological), or A/Hong Kong/1073/99(H9N2) (cat. no. 11229-V08H, Sino Biological) (0.5 μg/mL). Plates were blocked by 1% BSA in PBS at room temperature for 1 h. Serially diluted sera from individual mice were then incubated at 4°C for 16 to 18 h. Murine IgG was detected by incubation for 1 h with either horseradish peroxidase (HRP)-conjugated anti-mouse IgG (Fc specific) (1:5,000; cat. no. A2554, Merck, New Jersey, USA), biotinylated anti-mouse IgG1[a] (1:500; cat. no. 553500, BD Biosciences, New Jersey, USA), or biotinylated anti-mouse IgG2a[a] (1:500; cat. no. 553504, BD Biosciences). For biotinylated antibodies, a secondary incubation with HRP-conjugated streptavidin (1:5,000; cat.no. 7105-05, SouthernBiotech, Alabama, USA) at room temperature for 30 min was performed. The plates were developed by addition of 3,3′,5,5′-tetramethylbenzidine (TMB) solution (cat. no. CL07-1000ML, Merck), and the reaction was stopped after 10 min by addition of 1 M H2SO4. Absorbance at 450 nm was read using a Wallac EnVision 2104 Multilabel Reader (PerkinElmer, Massachusetts, USA).
Tjärnhage E., Brown D., Bogen B., Andersen T.K, & Grødeland G. (2023). Trimeric, APC-Targeted Subunit Vaccines Protect Mice against Seasonal and Pandemic Influenza. Journal of Virology, 97(2), e01694-22.
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Publication 2023
3,3',5,5'-tetramethylbenzidine Antibodies Biopharmaceuticals BLOOD Centrifugation Enzyme-Linked Immunosorbent Assay IGG-horseradish peroxidase IgG1 IgG2A Influenza in Birds isononanoyl oxybenzene sulfonate Mus Recombinant Proteins Serum Strep-avidin conjugated horseradish peroxidase Venipuncture Virus Vaccine, Influenza
3
ELISA for B. burgdorferi IgG Antibodies
In one study, blood was collected from anesthetized mice via cardiac puncture at the experimental endpoint, 28 days post-infection, and sera were obtained. B. burgdorferi-specific total IgG antibody titers were assessed by enzyme-linked immunosorbent assay (ELISA). ELISAs were prepared using sonicated B. burgdorferi strain B31-A3 organisms. Whole cell lysates were diluted to a final protein concentration of 0.15625 μg/mL in 0.2M sodium carbonate-bicarbonate buffer. Wells of a 96-well medium-binding polystyrene microtiter plate were coated with antigen and incubated for one hour. Following the coating step, wells were washed and then blocked by adding 300 μL of 2% bovine serum albumin in PBS and incubated at 4 °C overnight. After washing, the following were added sequentially to each well and incubated for one hour at room temperature, with washes between each step: 100 μL of serum serially diluted across the plate, beginning with a 1:200 dilution in the first well; 100 μL of 0.5 mg/mL biotinylated goat anti-mouse IgG Fc diluted 1:50,000 (Southern Biotech, Birmingham, AL, USA), and 100 μL of horseradish peroxidase-conjugated streptavidin diluted 1:2000 (Thermo Fisher Scientific, Waltham, MA, USA). Following this, wells were washed and then incubated with 100 μL 3,3′,5,5′-Tetramethylbenzidine for five minutes and the reaction stopped with 50 μL H2SO4. The optical density (OD) of each well was read at 450nm. Control wells consisted of no B. burgdorferi whole cell lysate; no serum; positive control serum from previously infected mice; negative control serum from uninfected mice; and no IgG Fc antibody. ELISA endpoints were determined by adding three times the standard deviation to the average of the OD readings from all background wells and were reported as the inverse of the last titer to be reported above this value [14 (link)].
Santiago K.N., Kozlik T., Liedhegner E.S., Slick R.A., Lawlor M.W, & Nardelli D.T. (2023). Effects of Regulatory T Cell Depletion in BALB/c Mice Infected with Low Doses of Borrelia burgdorferi. Pathogens, 12(2), 189.
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Publication 2023
3,3',5,5'-tetramethylbenzidine anti-IgG Antigens Bicarbonate, Sodium Bicarbonates BLOOD Buffers Carbonates Cells Enzyme-Linked Immunosorbent Assay Goat Heart Immunoglobulin G Infection Mus Polystyrenes Punctures Serum Serum Albumin, Bovine sodium carbonate Staphylococcal Protein A Strains Strep-avidin conjugated horseradish peroxidase Technique, Dilution Vision
4
Quantitative Immunohistochemical Analysis of GFAP in Dorsal Root Ganglia
To investigate the SGCs activation, L4-L6 DRG of three animals per group were dissected, post-fixed in 10% formalin for 3 h at RT and then paraffin embedded with HistoPro200 (HistoLine, Pantigliate, Milano, Italy). Three μm-thick serial slices were cut with a Leica RM2265 microtome (Microsystems GmbH, Wetzlar, Germany). Immunohistochemistry was performed using a rabbit polyclonal anti-glial fibrillary acid protein antibody (GFAP, Z0034, Dako Products-Agilent, Santa Clara, CA, USA). Paraffin sections were deparaffinized with xylene, rehydrated and antigens were retrieved with Proteinase K 20 ug/mL for 1 min at 37 °C. Immunolabeling was performed using an automatic Immunostainer (Autostainer 360, Epredia, Milano, Italy). Endogenous peroxidase activity was quenched by incubation in 3% H2O2 for 10 min at RT, then the slides were washed in PBS-Tween 0.5% and incubated in 5% NGS for 30 min at RT. The sections were incubated with anti-GFAP antibody (1:250 in 1% NGS) for 1 h at RT. Then, the slides were washed in PBS-Tween 0.5% and incubated with a biotinylated secondary antibody to rabbit IgG for 1 h at RT (1:200, Vector Laboratories, Peterborough, UK) followed by incubation with streptavidin-conjugated horseradish peroxidase for 1 h at RT (1:100, ABC kit Vectastain, Vector Laboratories, Peterborough, UK). The antigen–antibody complex was visualized by incubating the sections with 3.3-diaminobenzidine hydrochloride (DAB Substrate kit SK-4100, Vector Laboratories, Peterborough, UK). Negative controls were incubated only with the secondary antibody. Sections were counterstained with Haematoxylin and mounted in BioMount HM (BioOptica). Quantitative measure of GFAP-positive areas was performed for PTX and VEH PTX through Image J segmentation: three DRG/group were serially sectioned at a thickness of 3 μm and immunostained for GFAP. Stitched images were acquired, spaced at 12 μm, using a scanner (Zeiss Axioscan 7, Milano, Italy) and post-processed in order to erase GFAP-positive dorsal roots by using PhotoShop software. A segmentation of post-processed images was performed using a computer-assisted image analyzer (Trainable Weka Segmentation plugin of Image J software, US National Institutes of Health) trained to recognize GFAP-positive SGCs [31 (link)]. Image J classifier was applied to all images in the batch and the results were expressed as percentage of GFAP positive area/DRG total area.
Pozzi E., Ballarini E., Rodriguez-Menendez V., Canta A., Chiorazzi A., Monza L., Bossi M., Alberti P., Malacrida A., Meregalli C., Scuteri A., Cavaletti G, & Carozzi V.A. (2023). Paclitaxel, but Not Cisplatin, Affects Satellite Glial Cells in Dorsal Root Ganglia of Rats with Chemotherapy-Induced Peripheral Neurotoxicity. Toxics, 11(2), 93.
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Publication 2023
Animals anti-GFAP autoantibodies Antigens Cloning Vectors Complex, Immune Endopeptidase K Formalin Glial Fibrillary Acidic Protein Hematoxylin Immunoglobulins Immunohistochemistry Microtomy Paraffin Paraffin Embedding Peroxidase Peroxide, Hydrogen Rabbits Root, Dorsal Strep-avidin conjugated horseradish peroxidase Tweens Xylene
5
Quantification of Oxidative Stress Markers in Gastric Cancer
The concentration of malondialdehyde (MDA) in GC cells was detected by Lipid Peroxidation (MDA) Assay Kit (ab118970; Abcam, UK). GC cells were first cultivated with thiobarbituric acid (TBA) solution at 95°C for 1 h and then lysed with RIPA lysis buffer (C500005; Sangon). After the mixture was centrifuged (13,000 × g) at 4°C for 5 min, the supernatant was collected. Next, the supernatant and the standard were chilled in ice bath for 10 min. The samples were finally transferred to a new 96-well microplate and the OD value was calculated using an microplate ELISA reader at the wavelength of 532 nm.
The glutathione (GSH) level in GC cells was determined by GSH ELISA Kit (D751008; Sangon). The GC cells were washed with cold PBS and digested with trypsin (C0202; Beyotime). Post centrifugation at 1,000 × g for 5 min, cells were collected and washed with PBS three times. The supernatant was collected for detection following the resuspension of cells with PBS and the centrifugation at 1,500 × g for 10 min. The 50 µL of standard and supernatant were separately added to the standard well and sample wells and mixed with 50 µL of working fluid (100 µg/mL) created by the mixture of standard and standard/sample diluent 1, followed by incubation for 45 min. After the incubation, the working fluid was removed, and 350 µL of washing solution was added to every well for 2 min. Thereafter, the samples were incubated with 100 µL of horseradish peroxidase (HRP)-conjugated streptavidin working solution at 37°C for 30 min. Next, 300 µL of washing solution was used to wash each well four times. After staining with 90 µL of chromogenic agent at 37°C for 15 min without light, 50 µL of stop solution was used to terminate the reaction and the OD value was measured by an ELISA microplate reader at the wavelength of 450 nm.
Zhao H., Ding Y, & Zhang L. (2023). SIRT1/APE1 promotes the viability of gastric cancer cells by inhibiting p53 to suppress ferroptosis. Open Medicine, 18(1), 20220620.
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Publication 2023
azo rubin S Bath Biological Assay Buffers Centrifugation Cold Temperature Enzyme-Linked Immunosorbent Assay Light Lipid Peroxidation Malondialdehyde Radioimmunoprecipitation Assay Strep-avidin conjugated horseradish peroxidase thiobarbituric acid Trypsin

Top products related to «Strep-avidin conjugated horseradish peroxidase»

1
Horseradish peroxidase conjugated streptavidin by Thermo Fisher Scientific
Sourced in United States
Horseradish peroxidase-conjugated streptavidin is a protein complex that consists of the protein streptavidin covalently linked to the enzyme horseradish peroxidase. This complex can bind to biotin-labeled molecules and catalyze a colorimetric or chemiluminescent reaction when a suitable substrate is present.
2
Horseradish peroxidase conjugated streptavidin by Vector Laboratories
Sourced in United States
Horseradish peroxidase-conjugated streptavidin is a protein complex composed of streptavidin, a protein derived from the bacterium Streptomyces avidinii, and horseradish peroxidase, an enzyme extracted from the horseradish plant. The complex is designed for use in various biomedical and biochemical applications that involve the detection and visualization of biotinylated molecules.
3
Horseradish peroxidase conjugated streptavidin by BD
Sourced in United States
Horseradish peroxidase-conjugated streptavidin is a type of lab equipment used in various biotechnological and immunological applications. It is a conjugate composed of the streptavidin protein and the enzyme horseradish peroxidase. The core function of this product is to serve as a detection reagent, leveraging the high-affinity binding between streptavidin and biotin to enable signal amplification and visualization in assays and experiments.
4
Horseradish peroxidase hrp conjugated streptavidin by Thermo Fisher Scientific
Sourced in United States
Horseradish peroxidase (HRP)-conjugated streptavidin is a protein complex composed of streptavidin, a bacterial protein that binds to biotin, and horseradish peroxidase, an enzyme commonly used as a reporter in various immunoassays and detection methods. The HRP-conjugated streptavidin can be used to detect and quantify biotinylated molecules in a sample.
5
Bovine serum albumin (bsa) by Merck Group
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
6
Streptavidin conjugated horseradish peroxidase by R&D Systems
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Streptavidin-conjugated horseradish peroxidase is a protein-enzyme complex. Streptavidin, a bacterial protein, is covalently linked to horseradish peroxidase, an enzyme that catalyzes a chromogenic reaction. This product can be used for various bioassay and detection applications.
7
Horseradish peroxidase conjugated streptavidin by Agilent Technologies
Sourced in Denmark, China, United States
Horseradish peroxidase-conjugated streptavidin is a protein complex consisting of streptavidin, a protein derived from the bacterium Streptomyces avidinii, which is conjugated to the enzyme horseradish peroxidase. This complex facilitates the detection and visualization of biotinylated molecules in various biochemical and immunological applications.
8
3 3 diaminobenzidine (dab) by Agilent Technologies
Sourced in United States, Denmark, United Kingdom, Germany, Japan, Canada, China, France, Belgium, Netherlands, Poland
The DAB (3,3'-Diaminobenzidine) product from Agilent Technologies is a chromogenic substrate used in immunohistochemistry and immunocytochemistry applications. It provides a brown precipitate at the site of the antigen-antibody reaction, allowing for the visualization and localization of target proteins or antigens in biological samples.
9
Horseradish peroxidase conjugated streptavidin by Merck Group
Sourced in United States
Horseradish peroxidase-conjugated streptavidin is a protein complex composed of streptavidin, a tetrameric protein that binds to biotin, and horseradish peroxidase, an enzyme that catalyzes a colorimetric reaction. This complex can be used as a detection or labeling reagent in various bioanalytical techniques.
10
Biotinylated secondary antibody by Agilent Technologies
Sourced in Denmark, United States, Germany, United Kingdom, Japan
Biotinylated secondary antibody is a reagent used in immunoassays and other biochemical techniques. It binds to the primary antibody and is typically detected using a streptavidin-based detection system. The biotinylation allows for signal amplification, enhancing the sensitivity of the assay.

More about "Strep-avidin conjugated horseradish peroxidase"

Streptavidin-HRP conjugate, SA-HRP, avidin-biotin system, biotinylated secondary antibodies, diaminobenzidine (DAB), colorimetric detection, enzyme-linked immunoassays (ELISAs), western blotting, immunohistochemistry (IHC), immunocytochemistry, protein-protein interactions, affinity purification, high-sensitivity assays, signal amplification, reproducible research, experimental optimization, AI-driven literature review, PubCompare.ai.
Streptavidin-conjugated horseradish peroxidase (Strep-avidin-HRP) is a powerful tool widely used in a variety of biological applications.
This enzyme conjugate combines the exceptionally high-affinity binding of streptavidin and avidin with the versatile catalytic properties of horseradish peroxidase (HRP), enabling sensitive detection and amplification of target analytes.
The Strep-avidin-HRP system is a key component of the avidin-biotin technology, which is extensively utilized in enzyme-linked immunoassays (ELISAs), western blotting, immunohistochemistry (IHC), immunocytochemistry, and other affinity-based techniques.
Researchers can optimize their Strep-avidin-HRP protocols and experimental conditions using PubCompare.ai, an AI-driven platform that helps locate the best procedures from scientific literature, preprints, and patents.
This intelligent comparison tool empowers reproducible and accruate research by discovering the optimal products, reagents, and parameters for your next experiment.
By leveraging the power of PubCompare.ai, you can ensure your Strep-avidin-HRP-based assays and experiments achieve the highest sensitivity, specificity, and reliability.