Difference between revisions of "Part:BBa K4645001:Design"
Ruixuan Zhu (Talk | contribs) |
Ruixuan Zhu (Talk | contribs) |
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===Design Notes=== | ===Design Notes=== | ||
− | On the basis of the expression of functional target proteins, | + | On the basis of the expression of functional target proteins, His tag is added, which can help us better obtain high-purity target proteins. Additionally, an OmpA signaling peptide was fused to the N-terminus of NeuB to aid in its secretion to the periplasmic space for efficient antigen neutralization. |
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===Source=== | ===Source=== | ||
− | Velocimmune mice were immunized with recombinant dimeric Fel | + | Velocimmune mice were immunized with recombinant dimeric Fel d 1 and produced polyclonal antibodies.The amino acid sequence of one of the most effective monoclonal antibodies REGN 1908 was obtained through literature review. |
===References=== | ===References=== |
Latest revision as of 00:25, 12 October 2023
NeuA: scFv ( single-chain fragment variable)that inhibits the immune response to the feline
Assembly Compatibility:
- 10INCOMPATIBLE WITH RFC[10]Illegal EcoRI site found at 315
Illegal SpeI site found at 75 - 12INCOMPATIBLE WITH RFC[12]Illegal EcoRI site found at 315
Illegal SpeI site found at 75 - 21INCOMPATIBLE WITH RFC[21]Illegal EcoRI site found at 315
Illegal XhoI site found at 693 - 23INCOMPATIBLE WITH RFC[23]Illegal EcoRI site found at 315
Illegal SpeI site found at 75 - 25INCOMPATIBLE WITH RFC[25]Illegal EcoRI site found at 315
Illegal SpeI site found at 75 - 1000COMPATIBLE WITH RFC[1000]
Design Notes
On the basis of the expression of functional target proteins, His tag is added, which can help us better obtain high-purity target proteins. Additionally, an OmpA signaling peptide was fused to the N-terminus of NeuB to aid in its secretion to the periplasmic space for efficient antigen neutralization.
Source
Velocimmune mice were immunized with recombinant dimeric Fel d 1 and produced polyclonal antibodies.The amino acid sequence of one of the most effective monoclonal antibodies REGN 1908 was obtained through literature review.