M8896
Maltose–Agarose
buffered aqueous suspension, matrix 4% beaded agarose
form
buffered aqueous suspension
extent of labeling
~20 μmol per mL
matrix
4% beaded agarose
matrix activation
epichlorohydrin
matrix attachment
1-hydroxyl
matrix spacer
3 atoms
capacity
≥20 mg/mL binding capacity (concanavalin A)
storage temp.
2-8°C
Application
Maltose-agarose is used in protein chromatography, affinity chromatography and carbohydrate matrices. Maltose-agarose has been used to study surfactant protein D (SP-D), which plays an important role in innate immunity. Maltose-agarose has also been used to study numerous pathological mechanisms for diseases in the human lung, including Aspergillus fumigatus, a pathogenic fungus, and the human influenza A virus.
Physical form
Suspension in 0.01 M phosphate buffer, pH 6.8, containing 0.15 M NaCl and 0.02% thimerosal
Disclaimer
For U.S. Customers: Contains mercury; Do not place in trash - dispose according to local, state, or federal laws.
Storage Class
10 - Combustible liquids
wgk
WGK 1
Regulatory Information
新产品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Z Yang et al.
Thorax, 55(7), 579-584 (2000-06-17)
Aspergillus fumigatus is a pathogenic fungus which causes a range of diseases, particularly in the human lung. The pathological mechanism is unknown but may involve a complex mixture of biomolecules which can diffuse from the spore surface. This material is
Minoru Ujita et al.
Bioscience, biotechnology, and biochemistry, 73(1), 237-240 (2009-01-09)
Human macrophage dectin-1, a type II transmembrane beta-glucan receptor, was expressed as a fusion protein with an N-terminal hexahistidine tag and glutathione S-transferase in an Escherichia coli cell-free translation system, and assayed for binding specificity. Recombinant dectin-1 specifically bound to
C M Soerensen et al.
Immunology, 114(1), 72-82 (2004-12-21)
Surfactant protein D (SP-D) is a collectin believed to play an important role in innate immunity. SP-D is characterized by having a collagen-like domain and a carbohydrate recognition domain (CRD), which has a specific Ca(2+)-dependent specificity for saccharides and thus
U Kishore et al.
The Biochemical journal, 318 ( Pt 2), 505-511 (1996-09-01)
We have expressed the carbohydrate recognition domains (CRDs) of human lung surfactant protein D (SP-D) in Escherichia coli as a trimeric structure held together by the alpha-helical neck region of the molecule. The DNA sequence coding for the neck-region peptide
T P Hickling et al.
FEBS letters, 437(1-2), 65-69 (1998-11-06)
Lipopolysaccharide (LPS) induction of TNF-alpha release is a central event in the pathophysiology of gram-negative bacterial septicaemia. Lung surfactant protein A (SP-A) mediates pathogen/host cell interactions. Binding of SP-A to Pseudomonas aeruginosa LPS and the effects of SP-A with LPS
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