QSOX1
QSOX1 (quiescin sulfhydryl oxidase 1, also known as QSCN6) is a flavoprotein enzyme that introduces disulfide bonds into peptide and protein thiols. It contributes to the folding and assembly of extracellular proteins, including components of the extracellular matrix. Browse Assay Genie's current range of QSOX1 research reagents below, or read on for the biology behind the target.
QSOX1 catalyses the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides, reducing oxygen to hydrogen peroxide in the process. Through this activity it plays a role in disulfide bond formation in a variety of extracellular proteins. In fibroblasts, QSOX1 is required for normal incorporation of laminin into the extracellular matrix, and therefore for normal cell-cell adhesion and cell migration.
The QSOX1 gene encodes a protein that contains thioredoxin and ERV1 domains, members of two long-standing gene families. The protein belongs to the quiescin-sulfhydryl oxidase (QSOX) family and is classed by HGNC within the flavoproteins. UniProt records it at the Golgi apparatus membrane and as a secreted protein. Two transcript variants encoding two different isoforms have been reported for the human gene. Orthologous genes are named Qsox1 in both mouse and rat, which allows the enzyme to be studied in common rodent models.
The name reflects how the gene was first characterised. QSOX1 expression is induced as fibroblasts begin to exit the proliferative cycle and enter quiescence, which suggests a role in growth regulation. Earlier names include quiescin Q6 and quiescin Q6 sulfhydryl oxidase 1, and the alias QSCN6 is still found in the literature. Researchers studying QSOX1 therefore work at the interface of oxidative protein folding, extracellular matrix organisation and control of cell growth.
QSOX1 forms disulfide bonds in peptide and protein thiols, making it a useful enzyme for studying disulfide formation in extracellular proteins.
QSOX1 is required for normal laminin incorporation into the extracellular matrix in fibroblasts, linking it to matrix assembly.
Loss of QSOX1 function in fibroblasts affects cell-cell adhesion and cell migration, through its role in laminin incorporation.
QSOX1 expression rises as fibroblasts leave the proliferative cycle and enter quiescence, pointing to a role in growth regulation.
QSOX1 catalyses the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides, reducing oxygen to hydrogen peroxide. It contributes to disulfide bond formation in many extracellular proteins and, in fibroblasts, to laminin incorporation into the extracellular matrix, cell-cell adhesion and cell migration.
QSOX1 is also known as QSCN6, and earlier names were quiescin Q6 and quiescin Q6 sulfhydryl oxidase 1. UniProt lists the protein as sulfhydryl oxidase 1. Two transcript variants encoding two different isoforms have been described for the human gene.
Yes. Mouse and rat both carry an orthologous gene named Qsox1. The protein belongs to the quiescin-sulfhydryl oxidase family and contains thioredoxin and ERV1 domains. Check the datasheet of any product for its validated reactivity.
Other sulfhydryl oxidases, oxidative folding enzymes and extracellular matrix proteins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O00391; product specifications from Assay Genie datasheets.