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Recombinant Human HSP90β Fragment 2 produced in E. coli has a molecular mass of approximately 54 KDa.
The biological activity of GDNF is measured by its ability to support survival and stimulate neurite outgrowth of cultured embryonic chick dorsal root ganglia. Activity can also be measured by its ability to bind recombinant human GFRα1/Fc.
>95% as determined by SDS-PAGE.
Liquid. In PBS Buffer. Avoid freeze/thaw cycles.
Domain structure of the yeast heat-inducible Hsp90. Top: 3D structure of the dimeric Hsp90 based onPDB2CG9 coordinates. Bound ATP molecules are represented by space filling spheres. Bottom: 1D sequence of the yeast Hsp90. NTD= N-terminal domain (red), MD = middle domain (green), CTD = C-terminal domain (blue).
HSP90β Fragment 2 is the middle domain and c-terminal of HSP90β, it is his-tagged and expressed in E. coli.
ATP binding, RNA binding, calcium ion binding, low-density lipoprotein receptor binding, nucleotide binding, unfold protein binding, virion binding.