A9207
Avidin−Agarose from egg white
aqueous glycerol suspension
Synonym(s):
Avidin agarose
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About This Item
Recommended Products
biological source
egg white
Quality Level
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
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)
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Systematic evaluation of avidin-biotin interaction by fluorescence spectrophotometry
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The Biochemical Journal, 384(2), 385-390 (2004)
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