E32754
4,6-O-Ethylidene-α-D-glucose
Synonym(s):
4,6-O-Ethylidene α-D-glucopyranose, Ethylidene glucose, NSC 89726
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1 G
$103.00
About This Item
Empirical Formula (Hill Notation):
C8H14O6
CAS Number:
Molecular Weight:
206.19
EC Number:
MDL number:
UNSPSC Code:
12352200
PubChem Substance ID:
NACRES:
NA.22
Recommended Products
mp
168-170 °C (lit.)
SMILES string
CC1OC[C@H]2O[C@H](O)[C@H](O)[C@@H](O)[C@@H]2O1
InChI
1S/C8H14O6/c1-3-12-2-4-7(13-3)5(9)6(10)8(11)14-4/h3-11H,2H2,1H3/t3?,4-,5-,6-,7-,8+/m1/s1
InChI key
VZPBLPQAMPVTFO-NKWOADHPSA-N
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Y Oka et al.
The Journal of biological chemistry, 259(13), 8125-8133 (1984-07-10)
Irradiation of intact rat adipocytes with high intensity ultraviolet light in the presence of 0.5 microM [3H] cytochalasin B results in the labeling of Mr 43,000 and 46,000 proteins that reside in the plasma membrane fraction. In contrast to the
M Mueckler et al.
The Journal of biological chemistry, 269(32), 20533-20538 (1994-08-12)
The possible role of 5 transmembrane amino acid residues in the function of the Glut1 glucose transporter was investigated by site-directed mutagenesis. The residues were chosen based on their containing hydroxyl or amide side chains capable of hydrogen bonding to
M Hashiramoto et al.
The Journal of biological chemistry, 267(25), 17502-17507 (1992-09-05)
The structure-function relationship of the HepG2/erythrocyte-type glucose transporter (GLUT1) has been studied by in vitro site-directed mutagenesis. Chinese hamster ovary clones in which glucose transporters were transfected were shown by Western blotting with a GLUT1 anti-COOH-terminal peptide antibody to have
A F Gibbs et al.
The Biochemical journal, 256(2), 421-427 (1988-12-01)
Tryptic digestion has been used to investigate the conformational changes associated with substrate translocation by the human erythrocyte glucose transporter. The effects of substrates and inhibitors of transport on the rates of tryptic cleavage at the cytoplasmic surface of the
Y Yano et al.
The Biochemical journal, 295 ( Pt 1), 183-188 (1993-10-01)
The transport conformation of the human erythrocyte glucose transporter (GLUT1) modifies rates of proteolytic cleavage of this protein by a variety of enzymes. We investigated the effects of ligand-induced conformational change on the susceptibility to enzymic cleavage of the insulin-sensitive
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