Recombinant Human FGE protein is a Human Full Length protein, in the 34 to 374 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
>95% SDS-PAGE
< 1 EU/µg
HEK 293 cells
His tag C-Terminus
SDS-PAGE, HPLC
No
S Q E A G T G A G A G S L A G S C G C G T P Q R P G A H G S S A A A H R Y S R E A N A P G P V P G E R Q L A H S K M V P I P A G V F T M G T D D P Q I K Q D G E A P A R R V T I D A F Y M D A Y E V S N T E F E K F V N S T G Y L T E A E K F G D S F V F E G M L S E Q V K T N I Q Q A V A A A P W W L P V K G A N W R H P E G P D S T I L H R P D H P V L H V S W N D A V A Y C T W A G K R L P T E A E W E Y S C R G G L H N R L F P W G N K L Q P K G Q H Y A N I W Q G E F P V T N T G E D G F Q G T A P V D A F P P N G Y G L Y N I V G N A W E W T S D W W T V H H S V E E T L N P K G P P S G K D R V K K G G S Y M C H R S Y C Y R Y R C A A R S Q N T P D S S A S N L G F R C A A D R L P T M D V H H H H H H
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application HPLC | Reactivity Reacts | Dilution info - | Notes - |
Select an associated product type
Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins, using molecular oxygen and an unidentified reducing agent (PubMed:12757706, PubMed:15657036, PubMed:15907468, PubMed:16368756, PubMed:21224894, PubMed:25931126). 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile (PubMed:12757706, PubMed:15657036, PubMed:15907468, PubMed:16368756, PubMed:25931126). Known substrates include GALNS, ARSA, STS and ARSE (PubMed:12757706, PubMed:15657036, PubMed:15907468).
PSEC0152, UNQ3037/PRO9852, UNQ3037/PRO9852, PSEC0152, SUMF1, Formylglycine-generating enzyme, FGE, C-alpha-formylglycine-generating enzyme 1, Sulfatase-modifying factor 1
Recombinant Human FGE protein is a Human Full Length protein, in the 34 to 374 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
>95% SDS-PAGE
< 1 EU/µg
HEK 293 cells
His tag C-Terminus
SDS-PAGE, HPLC
No
No
Human
pH: 7.5
Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl, 0.02% Calcium chloride
S Q E A G T G A G A G S L A G S C G C G T P Q R P G A H G S S A A A H R Y S R E A N A P G P V P G E R Q L A H S K M V P I P A G V F T M G T D D P Q I K Q D G E A P A R R V T I D A F Y M D A Y E V S N T E F E K F V N S T G Y L T E A E K F G D S F V F E G M L S E Q V K T N I Q Q A V A A A P W W L P V K G A N W R H P E G P D S T I L H R P D H P V L H V S W N D A V A Y C T W A G K R L P T E A E W E Y S C R G G L H N R L F P W G N K L Q P K G Q H Y A N I W Q G E F P V T N T G E D G F Q G T A P V D A F P P N G Y G L Y N I V G N A W E W T S D W W T V H H S V E E T L N P K G P P S G K D R V K K G G S Y M C H R S Y C Y R Y R C A A R S Q N T P D S S A S N L G F R C A A D R L P T M D V H H H H H H
Full Length
38.2 kDa
34 to 374
Recombinant
His tag C-Terminus
Liquid
ab151647 was determined to be >95% pure by SEC-HPLC and reducing SDS-PAGE.
Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins, using molecular oxygen and an unidentified reducing agent (PubMed:12757706, PubMed:15657036, PubMed:15907468, PubMed:16368756, PubMed:21224894, PubMed:25931126). 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile (PubMed:12757706, PubMed:15657036, PubMed:15907468, PubMed:16368756, PubMed:25931126). Known substrates include GALNS, ARSA, STS and ARSE (PubMed:12757706, PubMed:15657036, PubMed:15907468).
Belongs to the sulfatase-modifying factor family.
N-glycosylated. Contains high-mannose-type oligosaccharides.
Blue Ice
-20°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
ab151647 was produced by a mammalian cell expression system in HEK293. This product was previously labelled as SUMF1
This supplementary information is collated from multiple sources and compiled automatically.
The FGE or Formylglycine-generating enzyme also known as SUMF1 plays a mechanical role by catalyzing the post-translational activation of sulfatases. This enzyme exists within the endoplasmic reticulum and possesses a molecular weight of approximately 35 kDa. FGE expression occurs broadly across various tissues reflecting its necessity for cellular function. Its action involves converting a specific cysteine residue to formylglycine in sulfatase enzymes essential for their functional activity.
Formylglycine-generating enzyme contributes significantly to the functionality of sulfatases which carry out essential steps in the degradation of sulfate-containing molecules. This conversion is not a part of a larger complex but enables critical activities through sulfatases. Sulfatases require formylglycine for activity highlighting FGE's role in regulating their presence and function within the cell.
Formylglycine-generating enzyme integrates within metabolic pathways involved in glycosaminoglycan degradation. Through this action it connects to proteins like arylsulfatases essential in hydrolyzing sulfate groups from complex carbohydrates. This hydrolysis occurs within the lysosomal degradation pathway where FGE-activated sulfatases function bridging metabolic processes important for cellular maintenance.
Mutations or deficiencies in formylglycine-generating enzyme lead to multiple sulfatase deficiency (MSD) a disorder affecting lysosomal function and causing progressive neurological damage. In this context alterations in this enzyme impact related proteins such as ARSA and other sulfatases disrupting normal catabolic processes and leading to the accumulation of sulfated compounds. Additionally FGE deficiencies connect to skeletal dysplasias illustrating the broad physiological impact this enzyme holds when its function is compromised.
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