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Methyl α d mannopyranoside mmp

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Methyl-α-D-mannopyranoside (MMP) is a monosaccharide derivative used as a laboratory reagent. It serves as a chemical building block for various applications in research and analysis. The core function of MMP is to provide a standardized carbohydrate molecule for experimental purposes.

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Lab products found in correlation

293fectin, by Thermo Fisher Scientific (2 mentions) Freestyle medium, by Thermo Fisher Scientific (2 mentions) Hek293f, by Thermo Fisher Scientific (2 mentions) Galanthus nivalis lectin, by Vector Laboratories (2 mentions) Superose 6 10 300 gl column, by GE Healthcare (2 mentions) Bicinchonic acid based assay, by Thermo Fisher Scientific (2 mentions) Bira enzyme, by Avidity (2 mentions) Vivaspin protein concentrator, by GE Healthcare (1 mentions) Phosphate buffered saline (pbs), by Lonza (1 mentions) Miracloth, by Merck Group (1 mentions) Stericup gp device, by Merck Group (1 mentions) Complete edta free protease inhibitor, by Roche (1 mentions) Dc protein assay, by Bio-Rad (1 mentions)

Close spelling variants of this product

Methyl α-D-mannopyranoside (26 citations) Methyl mannopyranoside (3 citations) α-methyl mannopyranoside (2 citations)

3 protocols using methyl α d mannopyranoside mmp

1

Purification of Engineered HIV-1 Envelope Glycoproteins

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BG505 SOSIP.664 gp140, BG505 SOSIP.664-His gp140, and BG505 SOSIP.664-avi gp140 were expressed in HEK293F (Invitrogen) as described previously14 (link). Briefly, HEK293F cells were maintained in FreeStyle medium (Invitrogen). For gp140 trimer production, HEK293F cells were seeded at a density of 0.5×106/mL. After 24 h, cells were transfected with 1 mg of 293Fectin (Invitrogen) with 300 μg of Env plasmid and 75 μg of furin plasmid in OPTI-MEM according to the manufacturer’s protocol. Supernatants were purified using a Galanthus nivalis lectin (Vector Labs) column and protein was eluted with 1M methyl-α-D-mannopyranoside (MMP, Sigma). Following buffer exchange into PBS, only trimers with AviTags were in vitro biotinylated using the BirA enzyme according to the manufacturer protocol (Avidity). The affinity-purified Env proteins were further purified to size homogeneity using size exclusion chromatography (SEC) on a Superose 6 10/300 GL column (GE Healthcare) in PBS. The trimer fractions were collected and pooled and protein concentrations were determined using either a bicinchonic acid-based assay (Thermo Scientific) or UV280 absorbance using theoretical extinction coefficients.
Sok D., Le K.M., Vadnais M., Saye-Francisco K., Jardine J.G., Torres J., Berndsen Z.T., Kong L., Stanfield R., Ruiz J., Ramos A., Liang C.H., Chen P.L., Criscitiello M.F., Mwangi W., Wilson I.A., Ward A.B., Smider V.V, & Burton D.R. (2017). Rapid elicitation of broadly neutralizing antibodies to HIV by immunization in cows. Nature, 548(7665), 108-111.
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2

Purification of Engineered HIV-1 Envelope Glycoproteins

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BG505 SOSIP.664 gp140, BG505 SOSIP.664-His gp140, and BG505 SOSIP.664-avi gp140 were expressed in HEK293F (Invitrogen) as described previously14 (link). Briefly, HEK293F cells were maintained in FreeStyle medium (Invitrogen). For gp140 trimer production, HEK293F cells were seeded at a density of 0.5×106/mL. After 24 h, cells were transfected with 1 mg of 293Fectin (Invitrogen) with 300 μg of Env plasmid and 75 μg of furin plasmid in OPTI-MEM according to the manufacturer’s protocol. Supernatants were purified using a Galanthus nivalis lectin (Vector Labs) column and protein was eluted with 1M methyl-α-D-mannopyranoside (MMP, Sigma). Following buffer exchange into PBS, only trimers with AviTags were in vitro biotinylated using the BirA enzyme according to the manufacturer protocol (Avidity). The affinity-purified Env proteins were further purified to size homogeneity using size exclusion chromatography (SEC) on a Superose 6 10/300 GL column (GE Healthcare) in PBS. The trimer fractions were collected and pooled and protein concentrations were determined using either a bicinchonic acid-based assay (Thermo Scientific) or UV280 absorbance using theoretical extinction coefficients.
Sok D., Le K.M., Vadnais M., Saye-Francisco K., Jardine J.G., Torres J., Berndsen Z.T., Kong L., Stanfield R., Ruiz J., Ramos A., Liang C.H., Chen P.L., Criscitiello M.F., Mwangi W., Wilson I.A., Ward A.B., Smider V.V, & Burton D.R. (2017). Rapid elicitation of broadly neutralizing antibodies to HIV by immunization in cows. Nature, 548(7665), 108-111.
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3

Plant-Derived Protein Purification

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The aerial parts of the plants were harvested 5 days post agroinfiltration and homogenized in two buffer volumes of PBS (Lonza), supplemented with cOmplete™ EDTA-free protease inhibitor (Roche). The crude homogenate was incubated for 1 h, at 4°C, with shaking and then filtered through four layers of Miracloth™ (Merck). The crude plant sap was then clarified by sequential centrifugation steps; twice at 15,344 × g for 20 min and then again at 17,000 × g for 20 min. The supernatant was vacuum-filtered through a 0.45 µM Stericup-GP device (Merck Millipore) and applied to a Galanthuis nivalis lectin (GNL) column (Sigma) with a 0.5–1 ml/min flow rate. The column was sequentially washed with 100 ml of 0.5 M NaCl and then 100 ml of PBS (Lonza). The proteins were eluted in 1 M methyl α-D-manno-pyranoside (MMP) (Sigma), buffer exchanged into PBS and then concentrated using a Vivaspin Protein Concentrator with a 30 kDa cut-off (GE Healthcare). The purified proteins were quantified using the DC™ Protein Assay (Bio-Rad).
Margolin E., Chapman R., Meyers A.E., van Diepen M.T., Ximba P., Hermanus T., Crowther C., Weber B., Morris L., Williamson A.L, & Rybicki E.P. (2019). Production and Immunogenicity of Soluble Plant-Produced HIV-1 Subtype C Envelope gp140 Immunogens. Frontiers in Plant Science, 10, 1378.
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