Difference between revisions of "Part:BBa T2012"
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This is a ''Strep''-tag tail domain designed to be at the C-terminus of a protein. ''Strep''-tags are typically used for detection, purification and immobilization of proteins. | This is a ''Strep''-tag tail domain designed to be at the C-terminus of a protein. ''Strep''-tags are typically used for detection, purification and immobilization of proteins. | ||
| − | Strep-tag specifically binds to core streptavidin. As the Strep-tag binds reversibly to the same pocket of streptavidin where the natural ligand D-biotin is complexed, it can be used to purify corresponding fusion proteins on affinity | + | ===Usage and Biology=== |
| − | columns with immobilized streptavidin. | + | Strep-tag specifically binds to core streptavidin. As the Strep-tag binds reversibly to the same pocket of streptavidin where the natural ligand D-biotin is complexed, it can be used to purify corresponding fusion proteins on affinity columns with immobilized streptavidin. |
Note that the ''Strep''-tag may only be used as a C-terminal tag. To address this limitation, the ''Strep''-tag II has been engineered for use as either an N- or C-terminal tag; however; it has slightly reduced binding affinity relative to the ''Strep''-tag. This shortcoming can be addressed at least in part by using the ''Strep''-Tactin protein, a variant of Streptavidin, which has been engineered to have higher affinity for both the ''Strep''-tag and ''Strep''-tag II peptides. [See references for details.] | Note that the ''Strep''-tag may only be used as a C-terminal tag. To address this limitation, the ''Strep''-tag II has been engineered for use as either an N- or C-terminal tag; however; it has slightly reduced binding affinity relative to the ''Strep''-tag. This shortcoming can be addressed at least in part by using the ''Strep''-Tactin protein, a variant of Streptavidin, which has been engineered to have higher affinity for both the ''Strep''-tag and ''Strep''-tag II peptides. [See references for details.] | ||
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Revision as of 19:59, 13 August 2009
Strep-tag tail domain (WRHPQFGG)
This is a Strep-tag tail domain designed to be at the C-terminus of a protein. Strep-tags are typically used for detection, purification and immobilization of proteins.
Usage and Biology
Strep-tag specifically binds to core streptavidin. As the Strep-tag binds reversibly to the same pocket of streptavidin where the natural ligand D-biotin is complexed, it can be used to purify corresponding fusion proteins on affinity columns with immobilized streptavidin.
Note that the Strep-tag may only be used as a C-terminal tag. To address this limitation, the Strep-tag II has been engineered for use as either an N- or C-terminal tag; however; it has slightly reduced binding affinity relative to the Strep-tag. This shortcoming can be addressed at least in part by using the Strep-Tactin protein, a variant of Streptavidin, which has been engineered to have higher affinity for both the Strep-tag and Strep-tag II peptides. [See references for details.]
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]