90572
D-Galactose-4-sulfat 钠盐
≥97.0% (TLC)
别名:
Gal-4S
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关于此项目
线性分子式:
C6H11O9SNa
化学文摘社编号:
分子量:
282.20
NACRES:
NA.25
PubChem Substance ID:
UNSPSC Code:
12352201
MDL number:
assay
≥97.0% (TLC)
storage temp.
−20°C
SMILES string
[Na+].OC[C@@H](O)[C@H](OS([O-])(=O)=O)[C@H](O)[C@@H](O)C=O
InChI
1S/C6H12O9S.Na/c7-1-3(9)5(11)6(4(10)2-8)15-16(12,13)14;/h1,3-6,8-11H,2H2,(H,12,13,14);/q;+1/p-1/t3-,4+,5+,6-;/m0./s1
InChI key
PPFRJSVPFMKACS-NQZVPSPJSA-M
Application
D-Galactose 4-sulfate (Gal-4S) may be used to help differentiate glycan sulfatide recognition/binding sites and to study the structure and biochemisty of carrageenans.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
法规信息
涉药品监管产品
此项目有
Rando Tuvikene et al.
Carbohydrate research, 344(6), 788-794 (2009-03-10)
The composition, structure, and thermal stability of carrageenans from unattached Coccotylus truncatus (the Baltic Sea, Estonia) were investigated. The complex polysaccharide was characterized by (13)C NMR and FTIR spectroscopy, ICP-OES and gel permeation chromatography methods. The main components of C.
S Yamada et al.
European journal of biochemistry, 233(2), 687-693 (1995-10-15)
The carbohydrate-protein linkage region of a chondroitin 4-sulfate chain attached to urinary trypsin inhibitor (UTI) was isolated from human urine and characterized structurally. The chondroitin 4-sulfate chain was released from UTI by beta-elimination using alkaline NaBH4 then digested with chondroitinase
T Barbeyron et al.
The Journal of biological chemistry, 275(45), 35499-35505 (2000-08-10)
iota-Carrageenases are polysaccharide hydrolases that cleave the beta-1,4 linkages between the d-galactose-4-sulfate and 3, 6-anhydro-d-galactose-2-sulfate residues in the red algal galactans known as iota-carrageenans. We report here on the purification of iota-carrageenase activity from the marine bacterium Zobellia galactanovorans and
Lena Jansson et al.
PloS one, 4(2), e4487-e4487 (2009-02-27)
The first step in the pathogenesis of enterotoxigenic Escherichia coli (ETEC) infections is adhesion of the bacterium to the small intestinal epithelium. Adhesion of ETEC is mediated by a number of antigenically distinct colonization factors, and among these, one of
Astrid Von Mentzer et al.
Virulence, 11(1), 381-390 (2020-04-05)
The ability to adhere via colonization factors to specific receptors located on the intestinal mucosa is a key virulence factor in enterotoxigenic Escherichia coli (ETEC) pathogenesis. Here, the potential glycosphingolipid receptors of the novel human ETEC colonization factor CS30 were
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