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Merck
CN

I4507

Sigma-Aldrich

2-Iminobiotin-Agarose

saline suspension

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MDL编号:
UNSPSC代码:
23151817
NACRES:
NA.56
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表单

saline suspension

基质

4% beaded agarose

基质活化

epoxy

基质附着

carboxy

基质隔离区

16 atoms

容量

≥4 mg/mL binding capacity (avidin)

储存温度

2-8°C

应用

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.

外形

Suspension in 0.5 M NaCl, 0.01 M sodium phosphate, pH 6.8, containing 0.02% sodium azide

储存分类代码

12 - Non Combustible Liquids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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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
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
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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