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CAN F 4 Protein, Canine, Recombinant (His)

产品编号 TMPY-05438

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.

CAN F 4 Protein, Canine, Recombinant (His)

CAN F 4 Protein, Canine, Recombinant (His)

产品编号 TMPY-05438
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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250 μg¥ 5,1005日内发货
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产品信息

生物活性
Activity testing is in progress. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
产品描述
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.
种属
Canine
表达系统
HEK293 Cells
标签C-His
蛋白编号D7PBH4
蛋白构建
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
蛋白纯度
> 90 % as determined by SDS-PAGE.
分子量19.1 kDa (predicted)
内毒素< 1.0 EU/μg of the protein as determined by the LAL method.
缓冲液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.
复溶方法
A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
存储
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°C. 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.
运输方式In general, Lyophilized powders are shipping with blue ice.
研究背景
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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