You Searched For: L(-)-Fucose

Supplier: Thermo Scientific Chemicals

Description: L-(-)-Fucose 99%

Certificates

Supplier: AFG Bioscience

Description: 2-Azido-2-deoxy-L-fucose ≥95%

Supplier: TCI America

Description: CAS Number: 3615-37-0
MDL Number: MFCD00135603
Molecular Formula: C6H12O5
Molecular Weight: 164.16
Purity/Analysis Method: >98.0% (HPLC)
Form: Crystal
Melting point (°C): 137
Specific rotation [a]20/D: 75 deg (C=1, H2O)

SDS Certificates

Supplier: AFG Bioscience

Description: 2-Deoxy-2-fluoro-L-fucose 95%

Supplier: AFG Bioscience

Description: 2-​Amino-​2-​deoxy-​L-​fucose HCl salt ≥95%

Supplier: TCI America

Description: CAS Number: 2438-80-4
MDL Number: MFCD00135607
Molecular Formula: C6H12O5
Molecular Weight: 164.16
Purity/Analysis Method: >97.0% (HPLC)
Form: Crystal
Melting point (°C): 140
Specific rotation [a]20/D: -75 deg (C=1, H2O)

SDS Certificates

Supplier: AFG Bioscience

Description: 2-Deoxy-2-fluoro-L-fucose, 3,4-diacetate 95%

Catalog Number: (TCL0169-1ML)

Supplier: TCI America

Description: Appearance: Colorless to Light yellow to Light orange clear liquid
Concentration(Lowry Methoed): 4.4 to 5.5 mg/mL
Molecular weight: 30000 ～ 40000(SDS-PAGE)
Hemagglutination activity: max. 15.6 micro g/mL(pH6.5)

SDS Certificates

Catalog Number: (75790-574)

Supplier: Prosci

Description: GDP-L-Fucose Synthase is a NADP(H)-binding protein

Catalog Number: (76699-980)

Supplier: AFG Bioscience

Description: Human L-Fucose Kinase(FUK) ELISA Kit

Catalog Number: (10087-138)

Supplier: Proteintech

Description: FPGT(Fucose-1-phosphate guanylyltransferase) is also named as GFPP. This protein catalyzes the formation of GDP-L-fucose from GTP and L-fucose-1-phosphate. It also functions as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids. FPGT has 6 isoforms produced by alternative splicing.

Catalog Number: (89319-104)

Supplier: Genetex

Description: Rabbit polyclonal antibody to FPGT (fucose-1-phosphate guanylyltransferase)

Supplier: New England Biolabs (NEB)

Description: a1-2,4,6 Fucosidase O is a broad specificity exoglycosidase that catalyzes the hydrolysis of terminal a1-2, a1-4 and a1-6 linked fucose residues from oligosaccharides. a1-2,4,6 Fucosidase O cleaves a1-6 fucose residues more efficiently than other linkages.

Catalog Number: (10102-988)

Supplier: Prosci

Description: LFNG is a member of the glycosyltransferase superfamily. It is a single-pass type II Golgi membrane protein that functions as a fucose-specific glycosyltransferase, adding an N-acetylglucosamine to the fucose residue of a group of signaling receptors involved in regulating cell fate decisions during development. Mutations in the gene that encodes this protein have been associated with autosomal recessive spondylocostal dysostosis 3. This gene encodes a member of the glycosyltransferase superfamily. The encoded protein is a single-pass type II Golgi membrane protein that functions as a fucose-specific glycosyltransferase, adding an N-acetylglucosamine to the fucose residue of a group of signaling receptors involved in regulating cell fate decisions during development. Mutations in this gene have been associated with autosomal recessive spondylocostal dysostosis 3. Alternatively spliced transcript variants that encode different isoforms have been described, however, not all variants have been fully characterized.

Catalog Number: (10355-112)

Supplier: Bioss

Description: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.

Catalog Number: (10087-198)

Supplier: Proteintech

Description: Fucosyltransferase 8 (FUT8) is GDP-fucose-glycoprotein fucosyltransferase and is localized in Golgi apparatus. FUT8 is involved in protein glycosylation by catalyzing the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans. FUT8 may be involved in human aging by regulating protein N-glycosylation and in the molecular pathogenesis of human pulmonary emphysema (PE).