This soluble and active alpha crystallin homolog from Methanococcoides burtonii was recombinantly produced in E. coli, posesses non-native protein salvage activity, and forms polydisperse complexes with anti aggregation properties.
Methanococcoides burtonii is a methylotrophic methanogenic archaeon which has adapted to live in temperatures that are permanantly at 1-2C. While the alpha-Crystallin Homolog (Mb sHSP) gene originated from a cold-adapted microorganism, it encodes a sHsp with extremely efficient and versatile chaperone activity, preventing protein aggregation or loss of enzyme activity even at elevated temperatures.
From the laboratory of Frank T. Robb, PhD, University of Maryland, Baltimore, Institute of Marine and Environmental Technology (IMET).
|Name:||alpha crystallin homolog Mb SHSP|
|Source:||E. coli BL21|
|Molecular Weight:||20 kDa|
|Amino Acid Sequence:||MKFGLVRRGSSDVSRWDPFDEIRQTQEHLNQLLREVSPFGGLFEGKSRAPLMDIKEEDNN VIVTTDLPGIDKEDVEISVNNNILEIHAEFKKESESEKEGYVQKERTYSSFSRSAVLPSV VSDEGVKAKLEAGVLTITLPKTKAEEKTKIKIE|
|Buffer:||HEPES 50 mM, pH7.5|
|Activity:||Protection of Bovine glutamate dehydrogenase at 42C|
|Suggested Amount per Experiment:||50 ng|
|Comments:||Stable to 60C|
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