Recombinant Human Sulfatase Modifying Factor 1/SUMF1 His Protein Summary
Description |
A denatured recombinant protein with a N-Terminal His-tag and corresponding to the amino acids 91-374 of Human Sulfatase Modifying Factor 1/SUMF1 Source: E.coli Amino Acid Sequence: MGSSHHHHHH SSGLVPRGSH MVPIPAGVFT MGTDDPQIKQ DGEAPARRVT IDAFYMDAYE VSNTEFEKFV NSTGYLTEAE KFGDSFVFEG MLSEQVKTNI QQAVAAAPWW LPVKGANWRH PEGPDSTILH RPDHPVLHVS WNDAVAYCTW AGKRLPTEAE WEYSCRGGLH NRLFPWGNKL QPKGQHYANI WQGEFPVTNT GEDGFQGTAP VDAFPPNGYG LYNIVGNAWE WTSDWWTVHH SVEETLNPKG PPSGKDRVKK GGSYMCHRSY CYRYRCAARS QNTPDSSASN LGFRCAADRL PTMD |
Source |
E. coli |
Protein/Peptide Type |
Recombinant Protein |
Gene |
SUMF1 |
Purity |
>85%, by SDS-PAGE |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
34.1 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles. |
Buffer |
20 mM Tris-HCl buffer (pH8.0), 2M UREA, 20% glycerol, 2 mM DTT |
Preservative |
No Preservative |
Concentration |
0.5 mg/ml |
Purity |
>85%, by SDS-PAGE |
Alternate Names for Recombinant Human Sulfatase Modifying Factor 1/SUMF1 His Protein
Background
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.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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