Skip to Content
Merck
All Photos(1)

Documents

A9207

Sigma-Aldrich

Avidin−Agarose from egg white

aqueous glycerol suspension

Synonym(s):

Avidin agarose

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

MDL number:
MFCD00130572
UNSPSC Code:
41106514
NACRES:
NA.56

biological source

egg white

conjugate

agarose conjugate

form

aqueous glycerol suspension

matrix

cross-linked 6% beaded agarose

matrix activation

epichlorohydrin

matrix attachment

amino

matrix spacer

15 atoms

storage temp.

−20°C

Related Categories

General description

Avidin comprises of 0.05% of total egg white protein. It is a glycosylated protein. It corresponds to a molecular weight of 16.5 kDa and exists as tetramer, which can bind a minimum of three biotin molecules.

Application

Avidin is used for the purification of biotin containing proteins, which can enhance cellular binding and internalization of the antibody (Ab)-functionalized capsules compared with control human immunoglobulin (IgG)-functionalized capsules, suggesting these capsules can specifically interact with cancer cells through antibody/antigen recognition.
Avidin-Agarose from egg white has been used:
  • in the precipitation of biotin tagged protein by pull down assay in neuroblastoma cell line (SH-SY5Y )
  • in the purification of Lewis(x) sugar binding proteins from Schistosoma mansoni
  • in avidin bead assay for purification of labelled biotin
  • for capture of glycoproteins from murine cornea samples

Biochem/physiol Actions

Avidin finds biotechnological applications due to its high-affinity ligand binding property. Avidin interaction with biotin through its carbohydrate chains is widely exploited in biotechnological applications. In cancer cells, avidin-biotin systems helps in the in vivo localization and drug targeting in tumor cells.

Unit Definition

One unit will bind 1.0 μg of d-biotin.

Physical form

Suspension in 50% glycerol, 0.01 M sodium phosphate, pH 7.0, containing 0.02% sodium azide.

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Amber L Jolly et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 31(6), 2393-2404 (2017-02-23)
Cell surface glycosylation is thought to be involved in barrier function against microbes at mucosal surfaces. Previously we showed that the epithelium of healthy mouse corneas becomes vulnerable to
Dielectric spectroscopy of molecular interactions based on the avidin-biotin complex
Mellor, B.L., et al.
Conference proceedings : Annual International Conference of the IEEE Engineering in Medicine and Biology Society, 3660-3663 (2011)
Covalent modification of cytoskeletal proteins in neuronal cells by tryptamine-4, 5-dione
Kato Y, et al.
Redox Biology, 2, 983-990 (2014)
Systematic evaluation of avidin-biotin interaction by fluorescence spectrophotometry
Sun, S., et al.
Spectrochimica Acta Part A: Molecular Spectroscopy, 89C, 99-104 (2011)
Efficient production of active chicken avidin using a bacterial signal peptide in Escherichia coli
Hytonen VP, et al.
The Biochemical Journal, 384(2), 385-390 (2004)
View All Related Papers

Related Content

Protein Pull-Down Techniques

Investigate in vitro protein-protein interactions with pull-down assays, utilizing affinity, GST pull-down, TAP, and co-immunoprecipitation methods.

Protein Pull-Down Techniques

Investigate in vitro protein-protein interactions with pull-down assays, utilizing affinity, GST pull-down, TAP, and co-immunoprecipitation methods.

Protein Pull-Down Techniques

Investigate in vitro protein-protein interactions with pull-down assays, utilizing affinity, GST pull-down, TAP, and co-immunoprecipitation methods.

Protein Pull-Down Techniques

Investigate in vitro protein-protein interactions with pull-down assays, utilizing affinity, GST pull-down, TAP, and co-immunoprecipitation methods.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service