Shop All NeutrAvidin Protein and Conjugates

Avidin, NeutrAvidin™, FITC conjugate Invitrogen™

Searching for superior alternatives to fluorescein? Our Alexa Fluor Dye Series offers everything you're looking for and more.

Avidin, NeutrAvidin™, Tetramethylrhodamine conjugate Invitrogen™

Our tetramethylrhodamine 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. The method used to deglycosylate the avidin retains its specific binding. This bright, orange-fluorescent reagent (absorption/emission maxima ~555/580 nm) is ideal for detecting biotinylated targets in fluorescence microscopy applications.

NeutrAvidin Protein Thermo Scientific™

Thermo Scientific™ NeutrAvidin Protein is a specially-prepared form of avidin that decreases background in biotin-binding.

Features include:
Near-neutral isoelectric point—pI = 6.3, more neutral than native avidin
Nearly devoid of glycosylation—decreased possibility of lectin binding compared to native avidin
No RYD recognition sequence—no known off-target binding domains like streptavidin
Affordable—significantly less expensive than streptavidin

NeutrAvidin Protein is deglycosylated native avidin from egg whites. Removal of the excess carbohydrate by an exclusive process yields a protein with a more neutral isoelectric point and less nonspecific binding properties. Purified NeutrAvidin Protein provides exceptional performance in western blot, ELISA, and IHC applications that require biotin-binding probes. Assay specificity, sensitivity, and signal-to-noise ratios with NeutrAvidin Protein are generally equivalent or better than with the significantly more expensive streptavidin.

Avidin is a glycoprotein found in the egg white and tissues of birds, reptiles, and amphibia. The biotin-binding protein contains four identical subunits having a combined mass of 67,000-68,000 daltons. Removing the glycosylation from avidin yields NeutrAvidin Protein with a mass of 60,000 daltons. Carbohydrate-based lectin binding is reduced to undetectable levels, yet biotin-binding affinity is retained. NeutrAvidin Protein offers the advantages of a neutral pI to minimize nonspecific adsorption, along with lysine residues that remain available for derivatization or other customized conjugation. NeutrAvidin Protein yields the lowest nonspecific binding among the known biotin-binding proteins. The specific activity for biotin binding is approximately 14 µg/mg of protein, which is near the theoretical maximum activity.

Related products
NeutrAvidin™ Protein, Horseradish Peroxidase Conjugated
NeutrAvidin™ Protein, Alkaline Phosphatase Conjugated
NeutrAvidin™ Protein, Fluorescein Conjugated
NeutrAvidin™ Protein, Maleimide-Activated

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. The method used to deglycosylate the avidin retains its specific binding.

NeutrAvidin Protein, HRP Thermo Scientific™

Thermo Scientific™ NeutrAvidin Protein-HRP is a specially-prepared form of avidin that decreases background in biotin-binding conjugated to peroxidase for substrate based detection.

Features include:
Near-neutral isoelectric point—pI = 6.3, more neutral than native avidin
Nearly devoid of glycosylation—decreased possibility of lectin binding compared to native avidin
No RYD recognition sequence—no known off-target binding domains like streptavidin
Affordable—significantly less expensive than streptavidin

NeutrAvidin Protein is deglycosylated native avidin from egg whites. Removal of the excess carbohydrate by an exclusive process yields a protein with a more neutral isoelectric point and less nonspecific binding properties. Purified and conjugated forms of NeutrAvidin Protein provide exceptional performance in western blot, ELISA, and IHC applications that require biotin-binding probes. Assay specificity, sensitivity, and signal-to-noise ratios with NeutrAvidin Protein are generally equivalent or better than with the significantly more expensive streptavidin.

Avidin is a glycoprotein found in the egg white and tissues of birds, reptiles, and amphibia. The biotin-binding protein contains four identical subunits having a combined mass of 67,000-68,000 daltons. Removing the glycosylation from avidin yields NeutrAvidin Protein with a mass of 60,000 daltons. Carbohydrate-based lectin binding is reduced to undetectable levels, yet biotin-binding affinity is retained. NeutrAvidin Protein offers the advantages of a neutral pI to minimize nonspecific adsorption, along with lysine residues that remain available for derivatization or other customized conjugation. NeutrAvidin Protein yields the lowest nonspecific binding among the known biotin-binding proteins. The specific activity for biotin binding is approximately 14µg/mg of protein, which is near the theoretical maximum activity.

Recommended applications: ELISA (assay dependent), immunohistochemistry (assay dependent), in situ hybridization (ISH) (assay dependent), western blot (assay dependent)

NeutrAvidin Protein, DyLight 680 Invitrogen™

NeutrAvidin for Western Blot, IF, ICC, IHC, IP, ELISA

Neutravidin Protein, DyLight 800 Invitrogen™

Neutravidin for Western Blot, IF, ICC, IHC, IP, ELISA

NeutrAvidin Protein, AP Thermo Scientific™

Thermo Scientific™ alkaline phosphatase-conjugated NeutrAvidin Protein is a specially-prepared form of avidin that decreases background in biotin-binding.

Features include:
Near-neutral isoelectric point—pI = 6.3, more neutral than native avidin
Nearly devoid of glycosylation—decreased possibility of lectin binding compared to native avidin
No RYD recognition sequence—no known off-target binding domains like streptavidin
Affordable—significantly less expensive than streptavidin

NeutrAvidin Protein is deglycosylated native avidin from egg whites. Removal of the excess carbohydrate by an exclusive process yields a protein with a more neutral isoelectric point and less nonspecific binding properties. Conjugated NeutrAvidin Protein provides exceptional performance in western blot, ELISA, and IHC applications that require biotin-binding probes. Assay specificity, sensitivity, and signal-to-noise ratios with NeutrAvidin Protein are generally equivalent or better than with the significantly more expensive streptavidin.

Avidin is a glycoprotein found in the egg white and tissues of birds, reptiles, and amphibia. The biotin-binding protein contains four identical subunits having a combined mass of 67,000-68,000 daltons. Removing the glycosylation from avidin yields NeutrAvidin Protein with a mass of 60,000 daltons. Carbohydrate-based lectin binding is reduced to undetectable levels, yet biotin-binding affinity is retained. NeutrAvidin Protein offers the advantages of a neutral pI to minimize nonspecific adsorption, along with lysine residues that remain available for derivatization or other customized conjugation. NeutrAvidin Protein yields the lowest nonspecific binding among the known biotin-binding proteins. The specific activity for biotin binding is approximately 14 µg/mg of protein, which is near the theoretical maximum activity.

Applications:
In situ hybridization—NeutrAvidin-AP Conjugate is currently being used by the Allen Institute for Brain Science to create the Allen Brain Atlas.
Western blotting—use NeutrAvidin Protein conjugates (HRP or AP) instead of streptavidin conjugates for detection of biotinylated target proteins or biotinylated primary or secondary antibodies in western blots.
ELISA—NeutrAvidin Protein conjugates (HRP or AP) replace corresponding streptavidin conjugates for direct or indirect sandwich ELISA detection schemes involving biotin-labeled proteins and antibodies. Depending on the specific assay components (e.g., blocking buffers, etc.), NeutrAvidin Protein conjugates provide similar or better assay performance measured as signal-to-noise ratio.

Related products
NeutrAvidin™ Protein
NeutrAvidin™ Protein, Horseradish Peroxidase Conjugated
NeutrAvidin™ Protein, Fluorescein Conjugated
NeutrAvidin™ Protein, Maleimide-Activated

Pierce™ High Sensitivity NeutrAvidin™-HRP Thermo Scientific™

Thermo Scientific Pierce High Sensitivity NeutrAvidin HRP Conjugate is a specially prepared peroxidase-conjugated form of avidin biotin-binding protein that provides signal amplification like poly-HRP and exceptional storage stability.

Features of High Sensitivity NeutrAvidin HRP Conjugate:

NeutrAvidin Protein—a specially deglycosylated form of avidin that provides highly specific, low-background binding of biotinylated antibodies in many applications.
High sensitivity—detect low levels of target without background; obtain high signal-to-noise ratios
Cost effective—use less conjugate in Western blotting and ELISA applications and still obtain excellent results
Flexible—compatible with typical chemiluminescent, fluorescent and colorimetric peroxidase substrates
Convenient—ready-to-use stabilized liquid format means there is no waiting for thawing and no need to aliquot

This specially-manufactured variety of HRP-conjugated avidin protein meets the demands of today's scientists for more sensitive detection in ELISA and Western blotting applications. The conjugate is suitable for use with chemiluminescent, chemifluorescent or colorimetric substrates. Each High Sensitivity HRP conjugate is packaged in an easy-to-use stabilized solution that enables convenient storage at 4°C for at least one year.

Our High Sensitivity HRP Conjugates outperform the competition on target detection, signal intensity and signal-to-noise ratios. For example, experiments indicate that the High Sensitivity Streptavidin-HRP can be diluted eight-to 10-fold more than traditional HRP conjugates and still produce similar results.

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. The method used to deglycosylate the avidin retains its specific binding. This bright, red-fluorescent reagent (absorption/emission maxima ~595/615 is ideal for detecting biotinylated targets in fluorescence microscopy applications.

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. The method used to deglycosylate the avidin retains its specific binding. This bright, fluorescent reagent is ideal for detecting biotinylated targets in flow cytometry applications.

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™, 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. The method used to deglycosylate the avidin retains its specific binding. This bright, red-fluorescent reagent (absorption/emission maxima ~570/590 nm) is ideal for detecting biotinylated targets in fluorescence microscopy applications.

NeutrAvidin Protein, DyLight 633 Invitrogen™

NeutrAvidin for Western Blot, IF, ICC, IHC, IP, ELISA

NeutrAvidin Protein, DyLight 594 Invitrogen™

NeutrAvidin for Western Blot, IF, ICC, IHC, IP, ELISA
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