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Human FUOM / Fucose mutarotase / FucM / C10orf125 Protein (His Tag)

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Human FUOM Protein Product Information
Synonym:C10orf125, FUOM
Protein Construction:A DNA sequence encoding the human C10orf125 (A2VDF0-1) (Met1-Leu154) was expressed with a polyhistidine tag at the N-terminus.
Expressed Host:E. coli
Shipping:In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Human FUOM Protein QC Testing
Purity:> 90 % as determined by SDS-PAGE
Endotoxin:Please contact us for more information.
Stability:Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N Terminal:His
Molecule Mass:The recombinant human C10orf125 consists of 169 amino acids and predicts a molecular mass of 18.6 KDa. It migrates as an approximately 19 KDa band in SDS-PAGE under reducing conditions.
Formulation:Lyophilized from sterile PBS, pH 7.4.
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Human FUOM Protein Usage Guide
Storage:Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution:A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Other FUOM Recombinant Protein Products
FUOM / fucose mutarotase / FucM Background

FUOM, also known as fucose mutarotase and FucM, belongs to the RbsD / FucU family. FUOM is involved in the interconversion between alpha- and beta-L-fucoses. L-Fucose has two isforms: alpha-L-fucose (29.5%) and beta-L-fucose (70.5%). The beta-form is metabolized through the salvage pathway. GDP-L-fucose formed either by the de novo or salvage pathways is transported into the endoplasmic reticulum, where it serves as a substrate for N- and O-glycosylations by fucosyltransferases. Fucosylated structures expressed on cell surfaces or secreted in biological fluids are believed to play a critical role in cell-cell adhesion and recognition processes. FUOM mainly exists as homodimer, but also functions as homotetramer, homooctamer, and homodecamer. FUOM's homodimeric form seems catalytically inactive.

Human FUOM / fucose mutarotase / FucM References
  • Deloukas P. et al., 2004, Nature. 429: 375-81.
  • Ota T. et al., 2004, Nat Genet. 36: 40-5.
  • Dongkyu Park. et al., 2007, Glycobiology. 17 (9): 955-62.
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    Catalog: 13974-H07E-20
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