SUMOproteinpurification

由 XF Zhou 著作 · 2020 · 被引用 9 次 — We describe a simple and rapid protein purification strategy in which the SUMO tag and Ulp1 protease are surface-displayed separately on Escherichia coli cells.

由 H Wang 著作 · 2010 · 被引用 102 次 — As a novel molecular chaperon domain, SUMO increases the yield of recombinant protein and makes it easier to dissolve in the soluble fraction ...

SUMO fusion technology for enhanced protein expression and purification in prokaryotes and eukaryotes. Heterologous Gene Expression in E.coli. Methods in ...

LifeSensors protein expression system has pioneered SUMO fusion technology, which increases the quantity and quality of numerous recombinant proteins.

2015年5月5日 — Either dialyze O/N or concentrate and dilute protein in cleavage buffer. If protein becomes cloudy, spin in tabletop centrifuge 4100 rpm, 15 min ...

Affinity purified anti-SUMO antibodies, developed in mouse, were conjugated to NHS-sepharose. It is an efficient technique for isolating recombinant proteins.

由 TR Butt 著作 · 2005 · 被引用 685 次 — SUMO fusion enhances protein expression, solubility, and purification in prokaryotes. Recently, SUMO has been fused to the N-terminus of several proteins ...

由 CD Lee 著作 · 2008 · 被引用 157 次 — This new system was shown to be effective for cloning, expression, and rapid purification of several difficult-to-produce authentic proteins.

由 F Guerrero 著作 · 2015 · 被引用 103 次 — We demonstrated that tandem-SUMO fusion vectors bearing five different fusion tags could improve solubility of otherwise poorly soluble protein fragments.

Sumo tag is most frequentely used as N-end fusion sequence in yeast to increase the expression and solubility of the desired recombinant protein.