Anti-Human SUMF1 Antibody Pair

Product Description: Sulfatase modifying factor 1 (SUMF1) is a glycosylated enzyme localized primarily in the endoplasmic reticulum (ER) and is essential for the post-translational activation of all eukaryotic sulfatases by converting a specific cysteine residue in their active site to C-alpha-formylglycine (FGly), a modification necessary for their catalytic activity. SUMF1 can also be secreted and subsequently taken up by cells, where it is trafficked back to the ER and remains functionally active, enhancing sulfatase activities in various tissues. Both glycosylated and non-glycosylated forms of SUMF1 can be secreted, but only the glycosylated form is efficiently internalized by cells through a receptor-mediated process. Mutations in the SUMF1 gene can disrupt FGly formation, leading to inactive sulfatases and causing multiple sulfatase deficiency (MSD), a rare lysosomal storage disorder characterized by the combined loss of function of all sulfatases, resulting in the accumulation of sulfated substrates and severe clinical symptoms. Protein 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) [The Uniprot Consortium]