Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • AccessionQ8NBK3
    • SpeciesHuman
    • SequenceMGSSHHHHHHSSGLVPRGSHMVPIPAGVFTMGTDDPQIKQDGEAPARRVT IDAFYMDAYEVSNTEFEKFVNSTGYLTEAEKFGDSFVFEGMLSEQVKTNI QQAVAAAPWWLPVKGANWRHPEGPDSTILHRPDHPVLHVSWNDAVAYCTW AGKRLPTEAEWEYSCRGGLHNRLFPWGNKLQPKGQHYANIWQGEFPVTNT GEDGFQGTAPVDAFPPNGYGLYNIVGNAWEWTSDWWTVHHSVEETLNPKG PPSGKDRVKKGGSYMCHRSYCYRYRCAARSQNTPDSSASNLGFRCAADRL PTMD
    • Molecular weight34 kDa including tags
    • Amino acids91 to 374
    • TagsHis tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab115708 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

  • Purity> 85 % SDS-PAGE.

  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.32% Tris HCl, 20% Glycerol, 0.03% DTT, 12.01% Urea

General Info

  • Alternative names
    • MGC150436
    • AAPA3037
    • C alpha formylglycine generating enzyme 1
    • C-alpha-formylglycine-generating enzyme 1
    • FGE
    • FGly generating enzyme
    • MGC131853
    • Sulfatase modifying factor 1 [Precursor]
    • Sulfatase-modifying factor 1
    • SUMF1
    • SUMF1_HUMAN
    • UNQ3037
    see all
  • FunctionUsing 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.
  • Tissue specificityUbiquitous. Highly expressed in kidney, pancreas and liver. Detected at lower levels in leukocytes, lung, placenta, small intestine, skeletal muscle and heart.
  • PathwayProtein modification; sulfatase oxidation.
  • Involvement in diseaseDefects in SUMF1 are the cause of multiple sulfatase deficiency (MSD) [MIM:272200]. MSD is a clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. Inheritance is autosomal recessive.
  • Sequence similaritiesBelongs to the sulfatase-modifying factor family.
  • Post-translational
    modifications
    N-glycosylated. Contains high-mannose-type oligosaccharides.
  • Cellular localizationEndoplasmic reticulum lumen.
  • Information by UniProt

Recombinant Human SUMF1 protein images

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

References for Recombinant Human SUMF1 protein (ab115708)

ab115708 has not yet been referenced specifically in any publications.

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