Difference between revisions of "Part:BBa T2012"

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.

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

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

@@ Line 2: / Line 2: @@
 <partinfo>BBa_T2012 short</partinfo>
-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
 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 might be overcome in part by using the ''Strep''-Tactin protein, a variant of Streptavidin, which has been engineered to have better peptide binding capacity.  [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.]
 <!-- Add more about the biology of this part here