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The catalytic sites of sulfatases are only active if they contain a unique amino acid, C-alpha-formylglycine (FGly). Additionally we are shipping SUMF2 Antibodies (12) and SUMF2 Proteins (5) and many more products for this protein.
SUMF2 interacted with IL-13 (show IL13 ELISA Kits) and inhibited IL-13 (show IL13 ELISA Kits) secretion in bronchial smooth muscle cells and lymphocytes, which was independent of IL-13 (show IL13 ELISA Kits) glycosylation
structural analysis of human pFGE by X-ray crystallography [pFGE]
pFGE (SUMF2) is the paralog of the Calpha (show PRKACA ELISA Kits)-formylglycine-generating enzyme
SUMF2 interacts with sulphatase-modifying factor 1 to regulate sulphatase activities.
pFGE is retained in the ER through its C-terminal tetrapeptide PGEL, a noncanonical variant of the classic KDEL ER-retention signal.
The catalytic sites of sulfatases are only active if they contain a unique amino acid, C-alpha-formylglycine (FGly). The FGly residue is posttranslationally generated from a cysteine by enzymes with FGly-generating activity. The gene described in this record is a member of the sulfatase-modifying factor family and encodes a protein with a DUF323 domain that localizes to the lumen of the endoplasmic reticulum. This protein has low levels of FGly-generating activity but can heterodimerize with another family member - a protein with high levels of FGly-generating activity. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
sulfatase modifying factor 2
, sulfatase-modifying factor 2
, Sulfatase-modifying factor 2
, C-alpha-formyglycine-generating enzyme 2
, C-alpha-formylglycine-generating enzyme 2
, paralog of the formylglycine-generating enzyme