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.
| 説明 |
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. |
| Species |
Canine
|
| Expression Host |
HEK293 Cells
|
| Tag |
C-His
|
| Accession Number |
D7PBH4
|
| Construction |
The canine Canf4 (NP_001177855.1) (Met1-Glu174) was expressed with a polyhistidine tag at the C-terminus.
|
| Protein Purity |
> 90 % as determined by SDS-PAGE.
|
| 分子量 |
19.1 kDa (predicted)
|
| Endotoxin |
< 1.0 EU/μg of the protein as determined by the LAL method.
|
| Formulation |
Lyophilized from a solution filtered through a 0.22 μm filter, containing 50 mM Tris, 100 mM NaCl, 0.02% TWeen 80, pH 8.0.Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization.
|
| Reconstitution |
A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
|
| Stability & Storage |
It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted protein solutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
|
| Shipping |
In general, Lyophilized powders are shipping with blue ice.
|
| Research Background |
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.
|
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