SuMF1, Recombinant Protein

Sulfatase modifying factor 1; FGE

For Research Use Only. Not for use in diagnostic procedures.

E Coli

> 85% by SDS-PAGE

Liquid. In 20mM Tris-HCl, pH8.0, 2M urea, 20%glycerol, 2mM DTT

0.5 mg/ml (determined by Bradford assay) (lot specific)

Can be stored at 4 degree C short term (1-2 weeks).
For long term storage, aliquot and store at -20 degree C or -70 degree C.
Avoid repeated freezing and thawing cycles.

Small volumes of SuMF1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

SuMF1 (Sulfatase-modifying factor 1) belongs to the SuMF family. SuMF1 is an enzyme that catalyzes the hydrolysis of sulfate esters by oxidizing a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue, which is also known as C-alpha-formylglycine. Mutations in this gene cause multiple sulfatase deficiency, a lysosomal storage disorder. Recombinant human SuMF1 protein, fused to His-tag at N-terminus, was expressed in E Coli.

Cytoskeleton

SDS-PAGE

34.1kDa (304aa)

sulfatase modifying factor 1

sulfatase-modifying factor 1

Sulfatase-modifying factor 1

FGE  [Similar Products]

This gene encodes an enzyme that catalyzes the hydrolysis of sulfate esters by oxidizing a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue, which is also known as C-alpha-formylglycine. Mutations in this gene cause multiple sulfatase deficiency, a lysosomal storage disorder. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2009]

Using molecular oxygen and an unidentified reducing agent, oxidizes a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue, which is also called C(alpha)-formylglycine. Known substrates include GALNS, ARSA, STS and ARSE.

Fraldi A., et al. (2007) Biochem J. 403 (2):305-12.; Cosma MP., et al. (2003) Cell 113 (4): 445-56.

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