Avidin is a glycoprotein with a molecular weight of approximately 62.4 kDa. Avidin is a biotin binding protein that shows high sequence homology in birds, reptiles and amphibians. Hen egg white avidin is a tetrameric protein composed of four identical subunits, each with the ability to bind biotin with high affinity and specificity (Kd ~ 1015 M). In biotechnology, the functional consequence of tetrameric biotin binding is signal amplification. Biotin-avidin bridging is a great way to increase signal strength while maintaining specificity. The sequence of avidin only shows 30% homology with streptavidin, and anti-avidin and anti-streptavidin antibodies are not immunologically cross reactive.
应用类型
ELISA,Immunohistochemistry,Western Blot,
免疫原
Avidin (Hen Egg White)
来源宿主
Rabbit
反应性
该【干冰】Anti-AVIDIN (Egg White) (RABBIT) Antibody - 200-4197S的详细信息查看Avidin is a glycoprotein with a molecular weight of approximately 62.4 kDa. Avidin is a biotin binding protein that shows high sequence homology in birds, reptiles and amphibians. Hen egg white avidin is a tetrameric protein composed of four identical subunits, each with the ability to bind biotin with high affinity and specificity (Kd ~ 1015 M). In biotechnology, the functional consequence of tetrameric biotin binding is signal amplification. Biotin-avidin bridging is a great way to increase signal strength while maintaining specificity. The sequence of avidin only shows 30% homology with streptavidin, and anti-avidin and anti-streptavidin antibodies are not immunologically cross reactive.提供的产品说明书。
保存建议
Store vial at -20° C or below prior to opening. This vial contains a relatively low volume of reagent (25 µL). To minimize loss of volume dilute 1:10 by adding 225 µL of the buffer stated above directly to the vial. Recap, mix thoroughly and briefly centrifuge to collect the volume at the bottom of the vial. Use this intermediate dilution when calculating final dilutions as recommended below. Store the vial at -20°C or below after dilution. Avoid cycles of freezing and thawing.