Hrp conjugated streptavidin

Manufactured by Proteintech

Sourced in United States

HRP-conjugated streptavidin is a protein that binds to biotin with high affinity. It is commonly used as a detection reagent in various immunoassays and blotting techniques.

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Lab products found in correlation

Bca protein assay kit, by Thermo Fisher Scientific (2 mentions) Goat anti mouse igm hrp, by Southern Biotech (1 mentions) Biotinylated habp, by Merck Group (1 mentions) Sialic acids, by Solarbio (1 mentions) Anti tgf β1, by LifeSpan BioSciences (1 mentions) Protease inhibitor cocktail, by MedChemExpress (1 mentions) Mouse monoclonal anti flag antibody, by Proteintech (1 mentions) Ibright imaging system, by Thermo Fisher Scientific (1 mentions) Pvdf membrane, by Merck Group (1 mentions) Anti gapdh antibody, by Proteintech (1 mentions) Pngase f, by New England Biolabs (1 mentions)

6 protocols using hrp conjugated streptavidin

Quantification of HAS2 Expression in Fascia

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Three isomers of HAS have been identified and highly conserved among mammalians (HAS1, HAS2, and HAS3), of which HAS2 plays a pivotal role. HAS2 knockout mice resulted in lethal in midgestation due to insufficient development of various organs, whereas other knockouts were not lethal.^{9 (link)} HAS2 also produces larger amount of HA faster than the others,^{24 (link)} which makes HAS2 important for wound repair. Therefore, we detected HAS2 immunoreactivity (ir) in the fascia. We also used hyaluronan-binding protein (HABP) due to its specificity to HA, whereas Alcian blue stains various types of acidic polysaccharides.
The frozen sections were washed with phosphate-buffered saline (PBS), blocked with 10% normal goat serum for 1 hour, incubated with anti-HAS2 (1:200, #sc-365263, Santa Cruz Laboratories, Santa Cruz, CA) or biotinylated HABP (1:250, Merck, Darmstadt, Germany) diluted in 1% normal goat serum incubation buffer overnight at 4°C. After repeated washes with PBS, the samples were incubated with the secondary antibody goat anti-mouse IgM-HRP (1:1000, SouthernBiotech, Birmingham, AL) for 2 hours or HRP-conjugated streptavidin (1:250, Proteintech, Rosemont, IL) for 30 minutes and washed in PBS. The reaction was then developed with 3,30-diaminobenzidine (DAB) and terminated with PBS. Cell quantification is expressed as the number of cells per field.

Wang R., Matsuoka Y., Sue N., Nakatsuka K., Tsuboi C, & Morimatsu H. (2023). Decreased expression of hyaluronan synthase and loss of hyaluronan-rich cells in the anterior tibial fascia of the rat model of chemotherapy-induced peripheral neuropathy. Pain Reports, 8(4), e1088.

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ELISA for Sialic Acid Binding

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The purified E protein was used in an enzyme-linked immunosorbent assay. The E protein (1 µg) was coated overnight at 4°C. The plates were blocked using 5% wt/vol BSA solution for 1 h at room temperature. The different concentrations of sialic acids (Solarbio) were added and incubated for 2 h. After washing, biotinylated SNA was added and incubated for 2 h. After washing again, HRP-conjugated streptavidin (Proteintech) was added to each well, and the plates were incubated for 1 h. The commercial peroxidase substrate system was used for signaling detection (SeraCare), and the optical density (OD) at 450 nm was measured with an ELISA reader.

He Y., Miao C., Yang S., Xu C., Liu Y., Zhu X., Wen Y., Wu R., Zhao Q., Huang X., Yan Q., Lang Y., Zhao S., Wang Y., Han X., Cao S., Hu Y, & Du S. (2024). Sialic acids as attachment factors in mosquitoes mediating Japanese encephalitis virus infection. Journal of Virology, 98(5), e01959-23.

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Evaluating Nsp9-Nb6 Interaction by ELISA

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The Nsp9-Nb6 interaction was evaluated by ELISA using 96-well microtiter plates coated with Nsp9 mutant protein (200 ng/well). After incubation with biotinylated Nb6, Nb-bound proteins were detected using horseradish peroxidase (HRP)-conjugated streptavidin (Proteintech, Wuhan, China) with wild type Nsp9 included as the control. Similarly, biotinylated wild type (WT) Nsp9 was utilized to test its binding to the Nb6 mutants.

Wang Y., Li R., Qiao S., Wang J., Liu H., Li Z., Ma H., Yang L., Ruan H., Weng M., Hiscox J.A., Stewart J.P., Nan Y., Zhang G, & Zhou E.M. (2020). Structural Characterization of Non-structural Protein 9 Complexed With Specific Nanobody Pinpoints Two Important Residues Involved in Porcine Reproductive and Respiratory Syndrome Virus Replication. Frontiers in Microbiology, 11, 581856.

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Immunohistochemical Analysis of TGF-β1 and pSmad2

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Immunohistochemical stainings were performed by labeled streptavidin biotin method without antigen retrieval. Briefly, endogenous peroxidase activities were inactivated by 0.3% hydrogen
peroxide methanol for 30 min and tissue non-specific binding sites were blocked using 5% normal goat serum. Tissue sections were overlaid with the 1:100 dilution of anti-TGF-β1 (LifeSpan
BioSciences, Inc., Seattle, WA, USA) or anti- pSmad2 (LifeSpan BioSciences, Inc.) and then incubated for overnight at 4°C. The tissue sections were washed in PBS buffer and then incubated
for 1 h with the 1:100 dilution of secondary goat anti-rabbit biotinylated antibodies (SouthernBioTech, Birmingham, AL, USA). The tissue sections were washed in PBS buffer and then incubated
for 1 h with the 1:500 dilution of HRP-conjugated Streptavidin (Proteintech Group, Inc., Rosemont, lL, USA) followed by peroxidase substrate, DAB reagent (Nacalai Tesque, Inc., Kyoto,
Japan). After optimal color development, tissue sections were immersed in sterile water, counterstained with hematoxylin or kernechtrot, and coverslipped. The levels of TGF-β1 and pSmad2
signals per sections were evaluated by an image analysis (WinROOF, Ver5.6, Mitani Co., Ltd., Tokyo, Japan).

Kobayashi H., Tachi A, & Hagita S. (2023). Time course of histopathology of bleomycin-induced pulmonary fibrosis using an intratracheal sprayer in mice. Experimental Animals, 73(1), 41-49.

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Competitive ELISA for nCoV Antibody Binding

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A competitive ELISA was used to test the competitive binding of nCoVmab1 and nCoVmab2 to the RBD, which could reveal the neutralization mechanism of the two antibodies. Briefly, hACE2-Fc was coated on a plate. nCoVmab1 and nCoVmab2 were fivefold serially diluted and mixed with biotinylated RBD at a fixed concentration of 0.25 nM. Then, the mixture was added to the hACE2-coated wells. HRP-conjugated streptavidin (Proteintech) was used as the secondary antibody. The following procedures were performed as described above.

Zhao S., Zhang H., Yang X., Zhang H., Chen Y., Zhan Y., Zhang X., Jiang R., Liu M., Liu L., Chen L., Tang W., Peng C., Gao X., Zhang Z., Shi Z, & Gong R. (2021). Identification of potent human neutralizing antibodies against SARS-CoV-2 implications for development of therapeutics and prophylactics. Nature Communications, 12, 4887.

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Cell Lysis and Protein Analysis

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The cells were lysed with ice-cold RIPA buffer (50 mM Tris-HCl pH 8.0, 150 mM NaCl, 0.1% SDS, 0.5% sodium deoxycholate, and 1% Triton X-100) containing 1× Protease Inhibitor Cocktail (MedChem Express, Monmouth Junction, USA). Cell lysates were clarified by centrifugation at 12,000 g for 10 min at 4°C. The protein concentration of lysates was quantified using a BCA Protein Assay kit (Thermo Fisher Scientific). Then, 20 μg of total protein or proteins which were treated with peptide-N-glycosidase F named PNGase F (New England Biolabs) or sialiase (New England Biolabs) was separated by 10% SDS-PAGE and transferred to PVDF membranes (Millipore, BIllerica, USA). After being blocked with 5% BSA, the biotinylated proteins were identified with HRP-conjugated streptavidin (1:5000; Proteintech). For the western blot analysis of
SpCBM, PVDF membrane was incubated with 20 μg/mL biotinylated
SpCBM. Immunoblotting was performed using a mouse monoclonal anti-FLAG antibody (1:1000; Proteintech) and anti-GAPDH antibody (1:5000; Proteintech). The membrane was incubated with HRP-conjugated AffiniPure goat anti-mouse IgG (H+L) secondary antibody (1:10,000; Proteintech). Protein detection was performed using the iBright imaging systems (Invitrogen, Carlsbad, USA).

Liu W., Long Y., Bao Y., Li Y., Deng M., Yang X., Zhu H, & Su Y. (2022). Efficient TurboID-based proximity labelling method for identifying terminal sialic acid glycosylation in living cells: New technique to identify sialic acid. Acta Biochimica et Biophysica Sinica, 54(12), 1841-1853.

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