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pHrodo™ Red Avidin (Fluorogenic pH Sensor) Invitrogen™
pHrodo™ Red Avidin is a conjugate of avidin and pHrodo™ Red dye, a novel, fluorogenic dye that dramatically increases in fluorescence as the pH of its surroundings become more acidic. pHrodo™ Red dye conjugates are non-fluorescent outside the cell, but fluoresce bright red in phagosomes, making them...

Avidin, from egg Thermo Scientific™
This Thermo Scientific brand product was originally part of the Alfa Aesar product portfolio. Some documentation and label information may refer to the legacy brand. The original Alfa Aesar product / item code or SKU reference has not changed as a part of the brand transition to Thermo Scientific.

Avidin, NeutrAvidin™ Biotin-binding Protein Invitrogen™
Our NeutrAvidin™ biotin-binding protein- a form of avidin that has been processed to remove carbohydrate and to lower its isoelectric point - can substantially decrease background due to nonspecific binding. The method used to deglycosylate the avidin retains its specific binding.

Avidin, NeutrAvidin™, Oregon Green™ 488 conjugate Invitrogen™
Our Oregon Green™ 488 conjugate of NeutrAvidin™ biotin-binding protein - a form of avidin that has been processed to remove carbohydrate and to lower its isoelectric point - can substantially decrease background due to nonspecific binding.

Avidin, Alexa Fluor™ 488 conjugate Invitrogen™
Our avidin, Alexa Fluor™ 488 conjugate is a bright, photostable probe with excitation and emission characteristics similar to those of fluorescein. Avidin is a glycosylated biotin-binding protein that has a basic isoelectric point and is widely used to detect biotinylated probes.

Avidin, NeutrAvidin™, PE conjugate Invitrogen™
Our R-phycoerythrin (R-PE) conjugate of NeutrAvidin® biotin-binding protein - a form of avidin that has been processed to remove carbohydrate and to lower its isoelectric point - can substantially decrease background due to nonspecific binding.

Avidin, NeutrAvidin™, Alexa Fluor™ 350 conjugate Invitrogen™
Our Alexa Fluor 350 conjugate of NeutrAvidin biotin-binding protein – a form of avidin that has been processed to remove carbohydrate and to lower its isoelectric point – can substantially decrease background due to nonspecific binding.

eBioscience™ Avidin HRP Invitrogen™
Avidin horseradish peroxidase is commonly used as a second step for the detection of biotinylated antibodies. Avidin is a glycoprotein from chicken egg whites that binds biotin with high affinity. Biotin is a tag that is frequently used to label antibodies and other probes for immunodetection...

Avidin, NeutrAvidin™, Texas Red™ conjugate Invitrogen™
Our Texas Red™ conjugate of NeutrAvidin™ biotin-binding protein - a form of avidin that has been processed to remove carbohydrate and to lower its isoelectric point - can substantially decrease background due to nonspecific binding.

Avidin, NeutrAvidin™, Horseradish Peroxidase conjugate Invitrogen™
Our horseradish peroxidase (HRP) conjugate of NeutrAvidin™ biotin-binding protein - a form of avidin that has been processed to remove carbohydrate and to lower its isoelectric point - can substantially decrease background due to nonspecific binding.

Avidin, Texas Red™ conjugate Invitrogen™
Our avidin, Texas Red™ conjugate is a bright, photostable probe with excitation and emission maxima ∼595/615. Avidin is a glycosylated biotin-binding protein that has a basic isoelectric point and is widely used to detect biotinylated probes.

Avidin, FITC conjugate Invitrogen™
Our avidin, fluorescein conjugate has excitation and emission maxima ∼494/518. Avidin is a glycosylated biotin-binding protein that has a basic isoelectric point and is widely used to detect biotinylated probes.

Avidin, Egg White Invitrogen™
Avidin from egg white is a glycosylated biotin-binding protein that has a basic isoelectric point and is widely used to detect biotinylated probes.

Avidin, NeutrAvidin™, Rhodamine Red™-X conjugate Invitrogen™
Our Rhodamine Red™-X conjugate of NeutrAvidin™ biotin-binding protein - a form of avidin that has been processed to remove carbohydrate and to lower its isoelectric point - can substantially decrease background due to nonspecific binding.