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Citations & References (13)
Invitrogen™
Avidin, NeutrAvidin™, Horseradish Peroxidase conjugate
Avidin, NeutrAvidin™, Horseradish Peroxidase conjugate
| Catalog Number | Quantity |
|---|---|
| A2664 | 1 mg |
Catalog number A2664
Price (USD)
253.00
Each
Quantity:
1 mg
Price (USD)
253.00
Each
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.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Label or DyeHRP (Horseradish Peroxidase)
Quantity1 mg
Shipping ConditionWet Ice
ConjugateHRP
Product LineNeutrAvidin
Unit SizeEach
Contents & Storage
Store in freezer (-5 to -30°C).
Citations & References (13)
Citations & References
Abstract
Suppression of nonspecific binding of avidin-biotin complex (ABC) to proteins electroblotted to nitrocellulose paper.
Journal:J Histochem Cytochem
PubMed ID:3772081
'Nitrocellulose blots of cell extracts reacted in sequence with biotinylated lectins and horseradish peroxidase-labeled avidin-biotin complex (ABC) often show considerable nonspecific staining of protein bands. Experiments were performed to determine which of the components of the ABC were responsible for this and whether or not the nature and ionic strength
Transmembrane topography of the 100-kDa a subunit (Vph1p) of the yeast vacuolar proton-translocating ATPase.
Journal:J Biol Chem
PubMed ID:10329659
'The membrane topography of the yeast vacuolar proton-translocating ATPase a subunit (Vph1p) has been investigated using cysteine-scanning mutagenesis. A Cys-less form of Vph1p lacking the seven endogenous cysteines was constructed and shown to have 80% of wild type activity. Single cysteine residues were introduced at 13 sites within the Cys-less
Artifactual detection of biotin on histones by streptavidin.
Journal:Anal Biochem
PubMed ID:17920026
'Biotinylation is a recent addition to the list of reported posttranslational modifications made to histones. Holocarboxylase synthetase (HCS) and biotinidase have been implicated as biotinylating enzymes. However, the details of the mechanism and the regulation of biotin transfer on and off histones remains unclear. Here we report that in a
Stimulation of the pentose phosphate pathway and glutathione levels by dehydroascorbate, the oxidized form of vitamin C.
Journal:FASEB J
PubMed ID:10877828
'Ascorbic acid, or vitamin C, generally functions as an antioxidant by directly reacting with reactive oxygen intermediates and has a vital role in defenses against oxidative stress. However, ascorbic acid also has pro-oxidant properties and may cause apoptosis of lymphoid and myeloid cells. The present study shows that dehydroascorbate, the
Improved immunocytochemical detection of biotinylated probes with Neutralite avidin.
Journal:Trends Genet
PubMed ID:8488564