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AB115708

Recombinant Human FGE protein (denatured)

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Recombinant Human FGE protein (denatured) is a Human Fragment protein, in the 91 to 374 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.

View Alternative Names

PSEC0152, UNQ3037/PRO9852, SUMF1, Formylglycine-generating enzyme, FGE, C-alpha-formylglycine-generating enzyme 1, Sulfatase-modifying factor 1

1 Images
SDS-PAGE - Recombinant Human FGE protein (denatured) (AB115708)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human FGE protein (denatured) (AB115708)

15% SDS-PAGE showing ab115708 at approximately 34.1kDa (3μg).

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q8NBK3

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 12.01% Urea, 0.32% Tris HCl, 0.03% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

This product was previously labelled as SUMF1
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMVPIPAGVFTMGTDDPQIKQDGEAPARRVTIDAFYMDAYEVSNTEFEKFVNSTGYLTEAEKFGDSFVFEGMLSEQVKTNIQQAVAAAPWWLPVKGANWRHPEGPDSTILHRPDHPVLHVSWNDAVAYCTWAGKRLPTEAEWEYSCRGGLHNRLFPWGNKLQPKGQHYANIWQGEFPVTNTGEDGFQGTAPVDAFPPNGYGLYNIVGNAWEWTSDWWTVHHSVEETLNPKGPPSGKDRVKKGGSYMCHRSYCYRYRCAARSQNTPDSSASNLGFRCAADRLPTMD","proteinLength":"Fragment","predictedMolecularWeight":"34.1 kDa","actualMolecularWeight":null,"aminoAcidEnd":374,"aminoAcidStart":91,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q8NBK3","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

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.
Biological function summary

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.

Pathways

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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Specifications

Form

Liquid

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General info

Function

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).

Sequence similarities

Belongs to the sulfatase-modifying factor family.

Post-translational modifications

N-glycosylated. Contains high-mannose-type oligosaccharides.

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Product protocols

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Target data

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).
See full target information SUMF1
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