Purified Human SUMF1 final product on SDS-PAGE under reducing (P+) and non-reducing (P-) conditions. The purity of Human SUMF1 appears to be greater than 95% based on reducing condition. The bands around 75 kDa in non-reducing is a dimer. The multiple bands at reducing conditions may be due to glycosylation and proteolytic truncation.
Cat #
Size
Price
Quantity
601801
25 ug
$145
601802
100 ug
$295
Product Details
Application
ELISA, BLI
Format
Liquid, Purified
Expression Host
HEK293
Target Name
SUMF1, Formylglycine-generating enzyme
Species
Human
accession number
Q8NBK3
Sources
Recombinant human SUMF1 protein (Ser34-Asp374) with C-terminus His tag was expressed in 293 Cells.
Molecular Weight
This protein has a predicted molecular weight of 38.8 kDa. Under DTT-reducing conditions, the protein migrates at approximately 40-45 kDa on SDS-PAGE.
Affinity Tag
C-His
Purity
>95% based on SDS-PAGE under reducing condition
Formulation
25 mM HEPES, 150 mM NaCl, 10% Glycerol, pH 7.4
Endotoxin level
Not tested
Protein Concentration
25µg size is bottled at 0.2mg/mL concentration. 100 µg size is supplied at a lot-specific concentration.
Storage and Handling
Briefly centrifuge the vial upon receipt. An unopened vial can be stored at 4°C for up to 2 weeks, or at -20°C or below for up to six months. The protein may be further diluted to 0.1 mg/mL using 0.22 µm-filtered HEPES buffer (pH 7.4). For long-term storage, the diluted stock solution should be aliquoted and stored at ≤ –70°C to minimize freeze-thaw cycles. If additional dilution is required, carrier proteins such as FBS or BSA should be added to maintain protein stability.
Background Information
Human SUMF1 (also known as formylglycine-generating enzyme, FGE) is a 42 kDa soluble glycoprotein located in the endoplasmic reticulum (ER) lumen. It activates sulfatases by converting a cysteine residue in their catalytic site into a formylglycine, a modification essential for sulfatase function. SUMF1 can form monomers, disulfide-linked homodimers, or heterodimers with SUMF2. It is a Ca²⁺-binding protein and exists in three splice isoforms. Mature human SUMF1 shares 90% amino acid identity with its mouse counterpart.
Purified Human SUMF1 final product on SDS-PAGE under reducing (P+) and non-reducing (P-) conditions. The purity of Human SUMF1 appears to be greater than 95% based on reducing condition. The bands around 75 kDa in non-reducing is a dimer. The multiple bands at reducing conditions may be due to glycosylation and proteolytic truncation.
