Details of the SBP
| General Information of Synthetic Binding Protein (SBP) (ID: SBP000331) | ||||||
|---|---|---|---|---|---|---|
| SBP Name |
ABD-derived affinity protein anti-TNF-alpha/HSA HT015
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| Synonyms |
ABD(HT015)
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| Molecular Weight | 5.0 kDa | |||||
| Design Method | Traditional methods (Site-directed mutagenesis and/or Directed evolution) | |||||
| Expression System | Escherichia coli | |||||
| Selection Method | Phage display and Staphylococcal surface display | |||||
| Highest Status | Research | |||||
| Sequence Length | 46 | |||||
| SBP Sequence |
>ABD-derived affinity protein anti-TNF-alpha/HSA HT015
LAGAKGFALEGLDNRGVSDYYKDLIDKAKTVEGVEALRKEILRALP |
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| 3D Structure | ||||||
| Computationally Modelled Structure | ||||||
| Click to Save PDB File | ||||||
| Template Name | Albumin-binding domain (ABD) | |||||
| Protein Scaffold Information of This SBP | ||||||
|---|---|---|---|---|---|---|
| Scaffold ID | PS001 | [1] | ||||
| Scaffold Name | ABD-derived affinity protein | |||||
| Scaffold Class | Non-Antibody | |||||
| Fold Type | Three Alpha-Helices | |||||
| Binding Target(s) of This SBP (BTS) |
|---|
| BTS Name | Details | Mechanism | Application | Affinity | Research Organization | Ref |
|---|---|---|---|---|---|---|
| Tumor necrosis factor | Binder | Research tool | Kd: 4.4 nM | Royal Institute of Technology; AlbaNova University Center | [1] | |
| Albumin | Binder | Research tool | Kd: 35 nM | Royal Institute of Technology; AlbaNova University Center | [1] | |