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Assay
≥97.0% (HPLC)
form
solid
optical activity
[α]/D 33.0±2.0°, c = 0.2 in H2O
color
beige
storage temp.
room temp
SMILES string
OC[C@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O
InChI
1S/C6H12O6/c7-1-3(9)5(11)6(12)4(10)2-8/h1,3-6,8-12H,2H2
InChI key
GZCGUPFRVQAUEE-UHFFFAOYSA-N
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Application
D-Altrose is used as a substrate to identify, differentiate and characterize aldose isomerases such as L-fucose isomerase from Caldicellulosiruptor saccharolyticus and d-Arabinose isomerase (d-AI) from Bacillus pallidus (B. pallidus) and Klebsiella pneumoniae.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Other Notes
To gain a comprehensive understanding of our extensive range of Monosaccharides for your research, we encourage you to visit our Carbohydrates Category page.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Yo-Han Ju et al.
Biotechnology letters, 32(2), 299-304 (2009-10-27)
A recombinant L-fucose isomerase from Caldicellulosiruptor saccharolyticus was purified as a single 68 kDa band with an activity of 76 U mg(-1). The molecular mass of the native enzyme was 204 kDa as a trimer. The maximum activity for L-fucose
Buetusiwa Thomas Menavuvu et al.
Journal of bioscience and bioengineering, 102(5), 436-441 (2006-12-26)
d-Arabinose isomerase from Klebsiella pneumoniae 40bXX was purified 12-fold with a 62.5% yield indicated by its electrophoretic homogeneity. The purified enzyme showed the highest activities toward d-arabinose and l-fucose as substrates at optimum conditions (50 mM glycine-NaOH, pH 9.0, 40
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