A9207
Avidin−Agarose from egg white
aqueous glycerol suspension
Synonym(s):
Avidin agarose
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About This Item
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
Regulatory Information
动植物源性产品
Certificates of Analysis (COA)
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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)
Yumi Abiko et al.
Free radical biology & medicine, 104, 118-128 (2017-01-04)
The current consensus is that environmental electrophiles activate redox signal transduction pathways through covalent modification of sensor proteins with reactive thiol groups at low concentrations, while they cause cell damage at higher concentrations. We previously exposed human carcinoma A431 cells
Senarath Dissanayake
Molecular immunology, 38(12-13), 911-919 (2002-05-16)
Fucosylated sugars in Schistosoma mansoni possess immunomodulatory properties. In order to gain insights to the mechanisms involved, attempts were made to identify host immune cell molecules that specifically recognize these sugars. On Western blots, specific binding of synthetic biotinylated fucose
Corneal surface glycosylation is modulated by IL-1R and Pseudomonas aeruginosa challenge but is insufficient for inhibiting bacterial binding
Jolly AL, et al.
Faseb Journal, 31(6), 2393-2404 (2017)
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)
Related Content
Investigate in vitro protein-protein interactions with pull-down assays, utilizing affinity, GST pull-down, TAP, and co-immunoprecipitation methods.
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