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Sulfo nhs xbiotin

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Sulfo-NHS-Xbiotin is a water-soluble biotin derivative used for labeling proteins. It contains a sulfo-N-hydroxysuccinimide (sulfo-NHS) ester group that can form covalent bonds with primary amine groups on proteins. The biotin moiety allows for detection or purification of labeled proteins using streptavidin-based systems.

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Lab products found in correlation

Alkaline phosphatase conjugated to streptavidin, by Vector Laboratories (2 mentions) Sigmafast p nitrophenyl phosphate tablets, by Merck Group (2 mentions)

2 protocols using sulfo nhs xbiotin

1

Virus-like Particle ELISA Assay

Check if the same lab product or an alternative is used in the 5 most similar protocols
Virus-like particles containing protease-purified Env trimers were prepared as previously described50 (link),51 (link),91 (link), and ELISAs on these VLPs were performed as described51 (link). Briefly, Immulon II plates were coated overnight at 4°C with VLPs at 20 times their concentration in transfection supernatants. Wells were washed with PBS and then blocked with 4% bovine serum albumin/10% fetal bovine serum in PBS. Various biotinylated monoclonal antibodies (biotinylated using sulfo-NHS-Xbiotin, Thermo), and CD4-IgG2 were then titrated in the presence or absence of a fixed concentration of 2μg/ml soluble CD4. Alkaline phosphatase conjugated to streptavidin (Vector Laboratories, Burlingame, CA; to detect biotinylated mAbs) or anti-Fc (Accurate, Westbury, NY; to detect CD4-IgG2) and SigmaFAST p-nitrophenyl phosphate tablets (Sigma) were then used to detect binding. Plates were read at 405 nm.
Kwon Y.D., Pancera M., Acharya P., Georgiev I.S., Crooks E.T., Gorman J., Joyce M.G., Guttman M., Ma X., Narpala S., Soto C., Terry D.S., Yang Y., Zhou T., Ahlsen G., Bailer R.T., Chambers M., Chuang G.Y., Doria-Rose N.A., Druz A., Hallen M.A., Harned A., Kirys T., Louder M.K., O’Dell S., Ofek G., Osawa K., Prabhakaran M., Sastry M., Stewart-Jones G.B., Stuckey J., Thomas P.V., Tittley T., Williams C., Zhang B., Zhao H., Zhou Z., Donald B.R., Lee L.K., Zolla-Pazner S., Baxa U., Schön A., Freire E., Shapiro L., Lee K.K., Arthos J., Munro J.B., Blanchard S.C., Mothes W., Binley J.M., McDermott A.B., Mascola J.R, & Kwong P.D. (2015). Crystal structure, conformational fixation, and entry-related interactions of mature ligand-free HIV-1 Env. Nature structural & molecular biology, 22(7), 522-531.
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2

Virus-like Particle ELISA Assay

Check if the same lab product or an alternative is used in the 5 most similar protocols
Virus-like particles containing protease-purified Env trimers were prepared as previously described50 (link),51 (link),91 (link), and ELISAs on these VLPs were performed as described51 (link). Briefly, Immulon II plates were coated overnight at 4°C with VLPs at 20 times their concentration in transfection supernatants. Wells were washed with PBS and then blocked with 4% bovine serum albumin/10% fetal bovine serum in PBS. Various biotinylated monoclonal antibodies (biotinylated using sulfo-NHS-Xbiotin, Thermo), and CD4-IgG2 were then titrated in the presence or absence of a fixed concentration of 2μg/ml soluble CD4. Alkaline phosphatase conjugated to streptavidin (Vector Laboratories, Burlingame, CA; to detect biotinylated mAbs) or anti-Fc (Accurate, Westbury, NY; to detect CD4-IgG2) and SigmaFAST p-nitrophenyl phosphate tablets (Sigma) were then used to detect binding. Plates were read at 405 nm.
Kwon Y.D., Pancera M., Acharya P., Georgiev I.S., Crooks E.T., Gorman J., Joyce M.G., Guttman M., Ma X., Narpala S., Soto C., Terry D.S., Yang Y., Zhou T., Ahlsen G., Bailer R.T., Chambers M., Chuang G.Y., Doria-Rose N.A., Druz A., Hallen M.A., Harned A., Kirys T., Louder M.K., O’Dell S., Ofek G., Osawa K., Prabhakaran M., Sastry M., Stewart-Jones G.B., Stuckey J., Thomas P.V., Tittley T., Williams C., Zhang B., Zhao H., Zhou Z., Donald B.R., Lee L.K., Zolla-Pazner S., Baxa U., Schön A., Freire E., Shapiro L., Lee K.K., Arthos J., Munro J.B., Blanchard S.C., Mothes W., Binley J.M., McDermott A.B., Mascola J.R, & Kwong P.D. (2015). Crystal structure, conformational fixation, and entry-related interactions of mature ligand-free HIV-1 Env. Nature structural & molecular biology, 22(7), 522-531.
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