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Description
Research Area
,Recombinant-Protein
Images & Validation
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| Application Notes |
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Key Properties
−| Expression System | HEK293 Cells |
|---|---|
| Biological Origin | Canine |
| Biological Activity | Dog dander is an important cause of respiratory allergy but its content of allergenic components is still incompletely known. The size and the amino acid composition of the ligand-binding pocket indicate that Can f 4 is capable of binding only relatively small hydrophobic molecules which are different from those that Can f 2 is able to bind. The crystal structure of Can f 4 contained both monomeric and dimeric forms of the allergen, suggesting that Can f 4 is able to form transient (weak) dimers. The existence of transient dimers in solution was confirmed by use of native mass spectrometry. The dimeric structure of Can f 4 is formed when the ends of four β-strands are packed against the same strands from the second monomer. |
| Tag | C-His |
| Expression Region | A DNA sequence encoding the canine Canf4 (NP_001177855.1) (Met1-Glu174) was expressed with a polyhistidine tag at the C-terminus. Predicted N terminal: Gln 17 |
| MW | 19.1 kDa (predicted) |
| Purity | 98.00% |
Storage & Handling
−| Storage | -20°C |
|---|---|
| Expiration Date | 6 months from date of receipt. |
| Disclaimer | For research use only |

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Quick Database Links
UniProt
UniProt Details
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Protocol Information
Protein Handling and Storage Guide
Protein Handling Guide