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form
saline suspension
matrix
4% beaded agarose
matrix activation
epoxy
matrix attachment
carboxy
matrix spacer
16 atoms
capacity
≥4 mg/mL binding capacity (avidin)
storage temp.
2-8°C
Application
2-Iminobiotin-agarose is an agarose conjugate in saline suspension used in affinity chromatography, protein chromatography and avidin biotin matrices. 2-Iminobiotin-agarose has been used to improve the development of vaccines.
Interaction with avidin is pH-dependent: forms a stable complex above pH 9.5 and dissociates at pH 4.
Physical form
Suspension in 0.5 M NaCl, 0.01 M sodium phosphate, pH 6.8, containing 0.02% sodium azide
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Piia Karisola et al.
The Journal of biological chemistry, 277(25), 22656-22661 (2002-03-23)
A novel approach to localize and reconstruct conformational IgE-binding epitope regions of hevein (Hev b6.02), a major natural rubber latex allergen, is described. An antimicrobial protein (AMP) from the amaranth Amaranthus caudatus was used as an immunologically non-IgE-binding adaptor molecule
Complexes of Streptavidin-Fused Antigens with Biotinylated Antibodies Targeting Receptors on Dendritic Cell Surface: A Novel Tool for Induction of Specific T-Cell Immune Responses.
Stanek, O., et al.
Molecular Biotechnology (2011)
O H Laitinen et al.
FEBS letters, 461(1-2), 52-58 (1999-11-24)
Sea urchin fibropellins are epidermal growth factor homologues that harbor a C-terminal domain, similar in sequence to hen egg-white avidin and bacterial streptavidin. The fibropellin sequence was used as a conceptual template for mutation of designated conserved tryptophan residues in
Vesa P Hytönen et al.
The Biochemical journal, 384(Pt 2), 385-390 (2004-08-25)
Chicken avidin is a highly popular tool with countless applications in the life sciences. In the present study, an efficient method for producing avidin protein in the periplasmic space of Escherichia coli in the active form is described. Avidin was
M H Qureshi et al.
The Journal of biological chemistry, 276(49), 46422-46428 (2001-10-05)
The strong biotin-streptavidin interaction limits the application of streptavidin as a reversible affinity matrix for purification of biotinylated biomolecules. To address this concern, a series of single, double, and triple streptavidin muteins with different affinities to biotin were designed. The
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