A5170
Anti-Avidin antibody produced in rabbit
whole antiserum
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About This Item
Produits recommandés
Source biologique
rabbit
Conjugué
unconjugated
Forme d'anticorps
whole antiserum
Type de produit anticorps
primary antibodies
Clone
polyclonal
Contient
15 mM sodium azide
Technique(s)
immunoelectrophoresis: suitable
indirect ELISA: 1:100,000
Conditions d'expédition
dry ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
unmodified
Description générale
Avidin is a homotetrameric glycoprotein found in the egg white of birds, reptiles and amphibians. Each subunit is 16 kDa, singly glycosylated and binds to a molecule of biotin with greater affinity and specificity. Recombinant avidin from corn is similar to avidin from egg white in terms of properties like isoelectric point (pI) and antigenic properties. Avidin from corn has low molecular weight than chicken egg-derived avidin. Commercial production of avidin from corn has certain advantages in terms of availability of greater biomass and avoiding the co-purification of animal virus.
Immunogène
avidin
Application
Anti-Avidin antibody produced in rabbit has been used in enzyme-linked immunosorbent assay (ELISA). It has also been used in preparation of antibody-Au nanoparticles.
The presence of Scavidin in BT4C glioma cells was assessed by western blot using a rabbit anti-avidin antibody as the primary at a dilution of 1:4000. Lehtolainen, P. (2002) Cloning and Characterization of Scavidin, a Fusion Protein for the Targeted Delivery of Biotinylated Molecules. J. Biol. Chem. 277:8545-8550.
Actions biochimiques/physiologiques
Avidin binds strongly to biotin. Thus, avidin-biotin association has been utilized in immunoassays to detect the localization of antigens in tissues. The use of avidin-biotin immunoassay enhances the sensitivity of the technique and facilitates the detection of antigens in low quantities.
Forme physique
Supplied as a liquid containing 15mM sodium azide as preservative
Notes préparatoires
treated to remove lipoproteins
Remarque sur l'analyse
This antisera is evaluated for performance and specificity by immunodiffusion and immunoelectrophoresis.
Clause de non-responsabilité
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
nwg
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
Coomassie Brilliant Dyes as Surface-Enhanced Raman Scattering Probes for Protein-Ligand Recognitions
Han, Xiao X. and others
Analytical Chemistry, 82(10), 4102-4106 (2010)
Commercial plant-produced recombinant avidin
Commercial Plant-Produced Recombinant Protein Products, 15-25 (2014)
Development of transgenic wheat (Triticum aestivum L.) expressing avidin gene conferring resistance to stored product insects
Abouseadaa HH, et al.
BMC plant biology, 15(1), 1-8 (2015)
Xiao X Han et al.
Analytical chemistry, 82(10), 4102-4106 (2010-04-24)
Coomassie brilliant dyes have high affinity to proteins and high Raman activity, and on the basis of which, we have employed brilliant blue R-250 (BBR) and brilliant blue G-250 (BBG) as surface-enhanced Raman scattering (SERS) labels to probe protein-ligand recognitions.
Colleen Murray et al.
Transgenic research, 19(6), 1041-1051 (2010-03-11)
The high affinity biotin-binding proteins (BBPs) avidin and streptavidin are established insecticidal agents, effective against a range of insect pests. Earlier work showed that, when expressed in planta, full length avidin and a truncated form of streptavidin are highly insecticidal.
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