Streptavidin hrp

Manufactured by Rockland Immunochemicals

Sourced in United States

Streptavidin-HRP is a conjugate of streptavidin, a protein that binds strongly to the vitamin biotin, and horseradish peroxidase (HRP), an enzyme that can catalyze a colorimetric reaction. This conjugate is commonly used in various immunoassay and detection techniques where the specific biotin-streptavidin interaction is leveraged.

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Lab products found in correlation

Multiskan fc, by Thermo Fisher Scientific (2 mentions) Tmb substrate solution, by Thermo Fisher Scientific (1 mentions) Protease inhibitor, by Merck Group (1 mentions) Ultracut uc7, by Leica camera (1 mentions) Rb anti iba1, by Fujifilm (1 mentions) Dab substrate kit, by Cell Marque (1 mentions) Ex 2 transmission electron microscope, by JEOL (1 mentions) Anti mouse ige, by BD (1 mentions) Biotin anti mouse ige, by BD (1 mentions) Anti mouse igg hrp, by Southern Biotech (1 mentions) Anti mouse iga hrp, by Southern Biotech (1 mentions) Tmb elisa substrate solution, by Thermo Fisher Scientific (1 mentions) Anti mouse igm hrp, by Southern Biotech (1 mentions) High binding eia ria 96 well plate, by Corning (1 mentions) Biotin anti human tnf α, by BioLegend (1 mentions) Avidin biotin blocking kit, by Vector Laboratories (1 mentions) Dab kit, by BD (1 mentions)

6 protocols using streptavidin hrp

Quantification of Chemokines in Tumors

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After digestion of E0771 tumors or naive mammary glands, protease inhibitors (Sigma-Aldrich) were added to the supernatant, which was stored at −80°C. Capture antibodies against mouse CCL19, CCL21, or CCL25 (R&D Systems) were diluted in 0.1 M NaHCO₃ and incubated at 4°C overnight. Plates were blocked with 3% BSA/PBS and incubated with tumor/mammary gland supernatant, followed by incubation with the respective biotinylated detection antibody against mouse CCL19, CCL21, or CCL25 (R&D Systems). Plates were then incubated with streptavidin-HRP (Rockland), developed with TMB Substrate solution (Thermo Fisher Scientific), stopped with 1M orthophosphoric acid, and read at 450 nm on a Biotrak II spectrophotometer (Amersham Biosciences).

Whyte C.E., Osman M., Kara E.E., Abbott C., Foeng J., McKenzie D.R., Fenix K.A., Harata-Lee Y., Foyle K.L., Boyle S.T., Kochetkova M., Aguilera A.R., Hou J., Li X.Y., Armstrong M.A., Pederson S.M., Comerford I., Smyth M.J, & McColl S.R. (2020). ACKR4 restrains antitumor immunity by regulating CCL21. The Journal of Experimental Medicine, 217(6), e20190634.

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Ultrastructural Analysis of Microglia

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Mice were perfused with 4 % PFA, brains were removed and immersion fixed. Brain sections were cut using a vibratome (100 μm) and incubated in 0.5 % gelatin, 5 % horse serum and 0.01 % saponin in PBS for 5 h. Microglia staining was performed using a Rb anti-Iba1 (1:600; Wako), a secondary biotinylated anti-Rb (1:500; Rockland), streptavidin-HRP (1:1000; Rockland, S000-03) for 3 h and visualized using DAB Substrate Kit (Cell Marque, 957D). Tissue was then fixed with 2 % PFA, 2.5 % GA and sections were processed using routine EM protocols. Grids were not counterstained to preserve immunostaining. Finished blocks were sectioned using a DiATOME ultra 45° diamond knife and a LEICA Ultracut UC7. Sections (90 nm) were cut and picked up onto 200 hex mesh, formvar-carbon coated copper grids (Ted Pella, 01800-F). Images were captured using a JEOL 1200 EX II Transmission Electron Microscope with AMT digital camera.

Cantoni C., Bollman B., Licastro D., Xie M., Mikesell R., Schmidt R., Yuede C.M., Galimberti D., Olivecrona G., Klein R.S., Cross A.H., Otero K, & Piccio L. (2015). TREM2 regulates microglial cell activation in response to demyelination in vivo. Acta neuropathologica, 129(3), 429-447.

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Enzyme Immunoassay for Antibody Detection

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High-binding EIA/RIA 96-well plates (Costar) were coated overnight with 10µg/mL BSA-NP₃₂ or BSA-NP₅ (Biosearch Technologies Inc) diluted in ELISA coating buffer (28.6mM Na₂Co₃, 11.9mM NaHCO_3, pH 9.6), or 2µg/mL anti-mouse IgE (BD 553413) diluted in PBS. Wells were subsequently washed four times with 0.05% Tween20/PBS, then blocked with 3% BSA/PBS for 2 hours at room temperature. After washing, sera was serially diluted in 1% BSA/PBS, added to wells and incubated for 2 hours at room temperature. Wells were washed and incubated with anti-mouse IgG-HRP (1030-05), anti-mouse IgM-HRP (1021-05), anti-mouse IgA-HRP (1040-05) from Southern Biotech, or anti-mouse IgE-biotin (BD 553419) diluted in 1% BSA/PBS for 2 hours at room temperature. Biotinylated antibodies were further incubated with streptavidin-HRP (Rockland) for 40 minutes at room temperature. After washing, HRP was detected with 1X TMB ELISA Substrate Solution (eBioscience) and color development was stopped with 1M orthophosphoric acid. Plates were analyzed at 450nm with a Biotrak II plate reader.

Bastow C.R., Kara E.E., Tyllis T.S., Vinuesa C.G., McColl S.R, & Comerford I. (2022). TFR Cells Express Functional CCR6 But It Is Dispensable for Their Development and Localization During Splenic Humoral Immune Responses. Frontiers in Immunology, 13, 873586.

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CCL20 Quantification in Mammary Tissue

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Wells were coated with anti-CCL20 capture antibody (R&D Systems) at 2 μg/ml overnight followed by a blocking step in PBS/3%BSA. Homogenized mammary tissue lysates (in PBS containing 10 % glycerol and 1x protease inhibitor) were added for 1.5 hours at 37 °C. Biotinylated anti-CCL20 detection antibody (R&D Systems) was added at 50 ng/ml for 1 hour at 37 °C followed by incubation with streptavidin-HRP (Rockland) for 30 minutes at room temperature. Wells were washed with PBS/0.05 % Tween after each incubation.

Boyle S.T., Faulkner J.W., McColl S.R, & Kochetkova M. (2015). The chemokine receptor CCR6 facilitates the onset of mammary neoplasia in the MMTV-PyMT mouse model via recruitment of tumor-promoting macrophages. Molecular Cancer, 14, 115.

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Quantitative Analysis of Human TNFα by ELISA

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Human TNFα was evaluated using recombinant TNFα (ELISA standard) (BioLegend), LEAF Purified anti-human TNFα (BioLegend), biotin-anti-human TNFα (BioLegend), streptavidin-HRP (horse radish peroxidase; Rockland, Limerick, PA, USA) and SIGMAFAST OPD (o-phenylenediamine dihydrochloride) tablets (Sigma-Aldrich). Briefly, high-binding 96-well plates were coated with 50 μl of the capture antibody and kept at 4 °C overnight. After washing, the wells were blocked with 200 μl of 2% bovine serum albumin-PBS for an hour. Samples and standards were incubated in the wells for 3 h and then detected using 50 μl of the biotin-conjugated antibodies. streptavidin-HRP antibodies were added after washing. The presence of cytokines was visualised using OPD tablets as a colorimetric substrate for HRP. The plates were then read at 490 nm using the MultiSkan FC (Thermo Fisher Scientific, Waltham, MA, USA) plate reader.

Garcia-Valtanen P., Guzman-Genuino R.M., Williams D.L., Hayball J.D, & Diener K.R. (2017). Evaluation of trained immunity by β-1, 3 (d)-glucan on murine monocytes in vitro and duration of response in vivo. Immunology and Cell Biology, 95(7), 601-610.

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Immunohistochemistry for P0 Protein

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5um FFPE sections were deparaffinized with xylene, rehydrated in descending concentrations of ethanol to water, and heat-mediated antigen retrieval in 0.1M citric acid pH 6. Sections were blocked for endogenous avidin and biotin (Avidin/Biotin Blocking Kit, Vector Laboratories, SP-2001) and for endogenous peroxidases using 3% hydrogen peroxide to reduce non-specific staining. Staining with rabbit anti-P0 (produced by the laboratory of author Dr. Bruce Trapp at Cleveland Clinic Lerner Research Institute) was performed by incubation 1:250 overnight at 4°C. A biotinylated secondary antibody (Rockland, 611-706-125) was applied for 1 hour at room temperature, followed by streptavidin-HRP (Rockland, S000-03). HRP was developed using a DAB kit (BD Pharmingen, 550880). Sections were then counterstained with Shandon Instant Hematoxylin Kit (Thermo, 6765015), dehydrated, and cover-slipped with Permount mounting medium. To be considered P0⁺, lesions had to show at least one P0⁺ axon.

Ghezzi L., Bollman B., De Feo L., Piccio L., Trapp B.D., Schmidt R.E, & Cross A.H. (2023). Schwann Cell Remyelination in the Multiple Sclerosis Central Nervous System. Laboratory investigation; a journal of technical methods and pathology, 103(6), 100128.

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