Recombinant Human Protein O-fucosyltransferase 1/POFUT1, CF

R&D Systems, part of Bio-Techne | Catalog # 7409-GT

R&D Systems, part of Bio-Techne
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Key Product Details

Learn more about Fluorescent Glycan Labeling and Detection

Source

NS0

Accession #

Q9H488

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Protein O-Fucosyltransferase 1/POFUT1 Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human Protein O-Fucosyltransferase 1/POFUT1 protein
Gly27-Leu384, with N-terminal HA (YPYDVPDYA) tag

Purity

>85%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Tyr (of HA tag)

Predicted Molecular Mass

42 kDa

SDS-PAGE

42-50 kDa, reducing conditions

Activity

Measured by its ability to hydrolyze the donor substrate GDP-fucose.
The specific activity is >0.5 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

7409-GT
Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Background: Protein O-Fucosyltransferase 1/POFUT1

Fucose is typically found as a terminal modification of branched chain glycoconjugates, but also exists in direct O-linkage to serine or threonine residues of a number of cell surface and secreted proteins (1, 2). O-fucose was originally identified from human urine (3) and subsequently from an EGF repeat of urinary-type plasminogen activator (uPA) (4). The consensus sequence for O-fucose modification was determined to be C2XXGGS/TC3, where C2 and C3 are the second and third conserved cysteine residues of the EGF repeat, X is any amino acid, and S/T is the modified serine or threonine (5). O-Fucose exists on glycoproteins as either a monosaccharide (Fuc-O-Ser/Thr), a tetrasaccharide (NeuAc alpha2, 3/6Gal beta1, 4GlcNAc beta1, 3Fuc-O-Ser/Thr), or a di- or trisaccharide intermediate in tetrasaccharide biosynthesis (5, 6). O-fucose glycans play important roles in Notch signaling (7). There are two protein O-fucosyltransferases, POFUT1 and POFUT2, and both enzymes are endoplasmic reticulum resident proteins with a short N-terminal cytoplasmic domain and a single pass transmembrane domain (type II membrane protein). For soluble expression of the protein, both the N-terminal transmembrane domain and the C-terminal ER retention sequence have been removed. POFUT1 is activated by manganese and has some hydrolase activity on the donor substrate GDP-Fucose. The hydrolase activity of the recombinant human POFUT1 was assayed using a malachite-based method (8).

References

  1. Martinez-Duncker, I. et al. (2003) Glycobiology 13:1c.
  2. Wang, Y. et al. (2001) ) J. Biol. Chem. 276:40338.
  3. Hallgren, P. et al. (1975) J. Biol. Chem. 250:5312.
  4. Kentzer, E.J. et al. (1990) Biochem. Biophys.Res. Commun. 171:401.
  5. Harris, R.J. and Spellman, M.W. (1993) Glycobiology 3:219.
  6. Moloney, D.J. et al. (2000) Nature 406:369.
  7. Stanley, P. and Guidos, C.J. (2009) Immunol. Rev. 230:201.
  8. Wu, Z.L. et al. (2011) Glycobiology 21:727.

Long Name

Protein O-fucosyltransferase 1/POFUT1

Alternate Names

FucT-1, FUT12, O-Fuc-T, O-FUT, POFUT1, Protein OFucosyltransferase 1

Entrez Gene IDs

23509 (Human); 140484 (Mouse); 311551 (Rat)

Gene Symbol

POFUT1

UniProt

Q9H488 (Human)

Additional Protein O-Fucosyltransferase 1/POFUT1 Products

Product Documents for Recombinant Human Protein O-fucosyltransferase 1/POFUT1, CF

Product Datasheets

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Product Specific Notices for Recombinant Human Protein O-fucosyltransferase 1/POFUT1, CF

Coomassie is a registered trademark of Imperial Chemical Industries Ltd.

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