Superose 6 increase 10 300 gl size exclusion chromatography

Manufactured by Cytiva

Superose 6 Increase 10/300 GL is a size-exclusion chromatography column designed for the separation and purification of biomolecules such as proteins, peptides, and nucleic acids. It features a prepacked, ready-to-use format with a bed volume of 24 mL and a separation range of 5,000 to 5,000,000 daltons.

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Lab products found in correlation

Complete his tag purification resin, by Roche (2 mentions) His tag purification resin, by Roche (1 mentions)

Close spelling variants of this product

Superose 6 Increase 10/300 GL Superose 6 Increase 10/300 Superose 6 10/300 GL Superose 6 10/300 Superose 6 Increase Superose 6

3 protocols using superose 6 increase 10 300 gl size exclusion chromatography

Purification of Stabilized SARS-CoV-2 Spike Ectodomain

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Protein expression and purification were performed as previously described (Hashiguchi et al., 2011 (link)). Briefly, the expression plasmid, pHLsec, encoding the BA.2.75 S ectodomain bearing six proline substitutions (F817P, A892P, A899P, A942P, K986P and V987P) (Hsieh et al., 2020 (link)) and the deletion of the furin cleavage site (i.e., RRAR to GSAG substitution) with a T4-fold trimerization domain or soluble human ACE2 ectodomain were transfected into HEK293S GnTI(-) cells. The proteins in the culture supernatant were purified with a cOmplete His-Tag Purification Resin (Roche, Cat# 5893682001) affinity column, followed by Superose 6 Increase 10/300 GL size-exclusion chromatography (Cytiva, Cat# 29091596) with calcium- and magnesium-free PBS buffer.

Saito A., Tamura T., Zahradnik J., Deguchi S., Tabata K., Anraku Y., Kimura I., Ito J., Yamasoba D., Nasser H., Toyoda M., Nagata K., Uriu K., Kosugi Y., Fujita S., Shofa M., Monira Begum M., Shimizu R., Oda Y., Suzuki R., Ito H., Nao N., Wang L., Tsuda M., Yoshimatsu K., Kuramochi J., Kita S., Sasaki-Tabata K., Fukuhara H., Maenaka K., Yamamoto Y., Nagamoto T., Asakura H., Nagashima M., Sadamasu K., Yoshimura K., Ueno T., Schreiber G., Takaori-Kondo A., Shirakawa K., Sawa H., Irie T., Hashiguchi T., Takayama K., Matsuno K., Tanaka S., Ikeda T., Fukuhara T, & Sato K. (2022). Virological characteristics of the SARS-CoV-2 Omicron BA.2.75 variant. Cell Host & Microbe, 30(11), 1540-1555.e15.

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Purification of SARS-CoV-2 XBB.1 Spike Ectodomain

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Protein expression and purification of XBB.1 S protein ectodomain and human ACE2 were performed as previously described^{10 (link)}. Briefly, the expression plasmid, pHLsec, encoding the XBB.1 S protein ectodomain bearing six proline substitutions (F817P, A892P, A899P, A942P, K986P and V987P)^{83 (link)} and the deletion of the furin cleavage site (i.e., RRAR to GSAG substitution) with a T4-foldon domain or soluble human ACE2 ectodomain were transfected into HEK293S GnTI(-) cells. Expressed proteins in the cell-culture supernatant were purified with a cOmplete His-Tag Purification Resin (Roche, Cat# 5893682001) affinity column, followed by Superose 6 Increase 10/300 GL size-exclusion chromatography (Cytiva, Cat# 29091596) with calcium- and magnesium-free PBS buffer.

Tamura T., Ito J., Uriu K., Zahradnik J., Kida I., Anraku Y., Nasser H., Shofa M., Oda Y., Lytras S., Nao N., Itakura Y., Deguchi S., Suzuki R., Wang L., Begum M.M., Kita S., Yajima H., Sasaki J., Sasaki-Tabata K., Shimizu R., Tsuda M., Kosugi Y., Fujita S., Pan L., Sauter D., Yoshimatsu K., Suzuki S., Asakura H., Nagashima M., Sadamasu K., Yoshimura K., Yamamoto Y., Nagamoto T., Schreiber G., Maenaka K., Hashiguchi T., Ikeda T., Fukuhara T., Saito A., Tanaka S., Matsuno K., Takayama K, & Sato K. (2023). Virological characteristics of the SARS-CoV-2 XBB variant derived from recombination of two Omicron subvariants. Nature Communications, 14, 2800.

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Purification of XBB.1.5 S Protein and ACE2

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The XBB.1.5 S protein ectodomain and human ACE2 were expressed and purified as previously described^{53 (link)}. Briefly, the expression plasmids, pHLsec, encoding the XBB.1.5 S protein ectodomain with six proline substitutions (F817P, A892P, A899P, A942P, K986P, and V987P)^{54 (link)} and deletion of the furin cleavage site (i.e., RRAR to GSAG substitution) with a T4-foldon domain or soluble human ACE2 ectodomain, were transfected into HEK293S GnTI(−) cells. Expressed proteins in the cell-culture supernatant were purified using a cOmplete His-Tag Purification Resin (Roche, Cat# 5893682001) affinity column, followed by Superose 6 Increase 10/300 GL size-exclusion chromatography (Cytiva, Cat# 29091596) with calcium- and magnesium-free PBS buffer.

Tamura T., Irie T., Deguchi S., Yajima H., Tsuda M., Nasser H., Mizuma K., Plianchaisuk A., Suzuki S., Uriu K., Begum M.M., Shimizu R., Jonathan M., Suzuki R., Kondo T., Ito H., Kamiyama A., Yoshimatsu K., Shofa M., Hashimoto R., Anraku Y., Kimura K.T., Kita S., Sasaki J., Sasaki-Tabata K., Maenaka K., Nao N., Wang L., Oda Y., Ikeda T., Saito A., Matsuno K., Ito J., Tanaka S., Sato K., Hashiguchi T., Takayama K, & Fukuhara T. (2024). Virological characteristics of the SARS-CoV-2 Omicron XBB.1.5 variant. Nature Communications, 15, 1176.

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