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Merck

A8706

Avidin from egg white

recombinant, expressed in corn, ≥12 units/mg protein (E1%/280)

Synonyme(s) :

AVID_CHICK

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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352202
EC Number:
215-783-6
NACRES:
NA.56
MDL number:
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Nom du produit

Avidin from egg white, recombinant, expressed in corn, ≥12 units/mg protein (E1%/280)

recombinant

expressed in corn

assay

≥80% protein basis (biuret)

form

powder

specific activity

≥12 units/mg protein (E1%/280)

mol wt

glycoprotein 66 kDa
subunit 16 kDa

technique(s)

ELISA: suitable
immunoblotting: suitable
immunoelectrophoresis: suitable

UniProt accession no.

storage temp.

2-8°C

Quality Level

Gene Information

chicken ... AVD(396260)

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Application

Avidin egg white was used in an assay using functionalized xenon as a biosensor to detect biotin-avidin binding. Egg white was used at 80 nmol.
Avidin forms an extremely strong complex with d-biotin (Kd ~ 10-15). This activity has made both avidin and biotin extremely useful labels in immunochemical methods of detection and quantitation.

General description

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 except for the molecular weight. Avidin from corn has low molecular weight than chicken egg-derived avidin. This might be due to less complex glycosylation composition in plants. Commercial production of avidin from corn has certain advantages in terms of availability of greater biomass and avoiding the co-purification of animal virus.

Other Notes

One unit will bind 1.0 μg of d-biotin.

Preparation Note

Affinity purified

Classe de stockage

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Biopharmaceuticals in Plants: Toward the Next Century of Medicine, 121-122 (2009)
Tom J A Kokhuis et al.
Ultrasound in medicine & biology, 39(3), 490-506 (2013-01-26)
In this study, we investigated the effect of secondary Bjerknes forces on targeted microbubbles using high-speed optical imaging. We observed that targeted microbubbles attached to an underlying surface and subject to secondary Bjerknes forces deform in the direction of their
Ray C Schmidt et al.
Biomaterials, 34(15), 3758-3762 (2013-03-05)
The avidin-biotin system is a highly specific reaction that has been used in a wide range of biomedical applications, including surface modification and cell patterning. We systematically examined a number of avidin derivatives as the basis for a simple and
Commercial Plant-Produced Recombinant Protein Products, 15-25 (2014)
Sofia H L Frost et al.
Cancer biotherapy & radiopharmaceuticals, 28(2), 108-114 (2012-12-13)
Abstract Purpose: Pretargeted radioimmunotherapy (PRIT) against intraperitoneal (i.p.) ovarian microtumors using avidin-conjugated monoclonal antibody MX35 (avidin-MX35) and (211)At-labeled, biotinylated, succinylated poly-l-lysine ((211)At-B-PLsuc) was compared with conventional radioimmunotherapy (RIT) using (211)At-labeled MX35 in a nude mouse model. Mice were inoculated i.p.

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