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A8706

Sigma-Aldrich

Avidin from egg white

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

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Synonym(s):
AVID_CHICK
CAS Number:
EC Number:
MDL number:
NACRES:
NA.56

recombinant

expressed in corn

Quality Level

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

Gene Information

chicken ... AVD(396260)

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This Item
A9275A2050A7294
Sigma-Aldrich

A8706

Avidin from egg white

Sigma-Aldrich

A9275

Avidin from egg white

Avidin–FITC from egg white buffered aqueous solution

A2050

Avidin–FITC from egg white

Avidin–Alkaline Phosphatase buffered aqueous solution

A7294

Avidin–Alkaline Phosphatase

recombinant

expressed in corn

recombinant

-

recombinant

-

recombinant

-

assay

≥80% protein basis (biuret)

assay

≥98% (SDS-PAGE)

assay

-

assay

-

form

powder

form

lyophilized powder

form

buffered aqueous solution

form

buffered aqueous solution

mol wt

glycoprotein 66 kDa, subunit 16 kDa

mol wt

glycoprotein 66 kDa, subunit 16 kDa

mol wt

-

mol wt

-

Gene Information

chicken ... AVD(396260)

Gene Information

-

Gene Information

chicken ... AVD(396260)

Gene Information

-

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.

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.

Unit Definition

One unit will bind 1.0 μg of d-biotin.

Preparation Note

Affinity purified

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Stefan Schillberg et al.
Journal of plant physiology, 258-259, 153359-153359 (2021-01-19)
Recombinant proteins play an important role in many areas of our lives. For example, recombinant enzymes are used in the food and chemical industries and as high-quality proteins for research, diagnostic and therapeutic applications. The production of recombinant proteins is
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.
The avidin-biotin complex (ABC) method and other avidin-biotin binding methods.
G L Bratthauer
Methods in molecular biology (Clifton, N.J.), 115, 203-214 (1999-03-31)
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

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