Abcam, ab313611, Human GALNT7 ELISA

Size: 1 x 96Tests
Human GALNT7 ELISA is a Sandwich (quantitative) ELISA for the measurement of Human GALNT7 ELISA in Human in Cell Culture Media, Biofluids samples.
Key facts
Detection method:Colorimetric,
Sample types:Cell culture supernatant, Plasma, Serum,
Reacts with:Human,
Assay type:Sandwich (quantitative),
Sensitivity:= 22 pg/mL,
Range:22 - 5000 pg/mL,
Assay Platform:Pre-coated microplate (12 x 8 well strips)

Product details:
Human GALNT7 ELISA kit is an
in vitro
enzyme-linked immunosorbent assay for the quantitative measurement of human GALNT7 in serum, plasma and cell culture supernatants. This assay employs an antibody specific for human GALNT7 coated on a 96-well plate.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information--20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
GALNT7 also known as polypeptide N-acetylgalactosaminyltransferase 7 is an enzyme involved in the initial step of O-glycosylation. This process involves the transfer of N-acetylgalactosamine (GalNAc) to serine or threonine residues on proteins. GALNT7 weighs approximately 72 kilodaltons and belongs to the family of GalNAc-transferases. The expression of GALNT7 is widespread predominantly found in the liver and pancreas but is also present in other tissues.
Biological function summary
GALNT7 catalyzes the addition of GalNAc to proteins in the Golgi apparatus. This modification is important for mucin-type O-glycan biosynthesis which influences protein folding stability and cellular signaling. GALNT7 does not function as part of a large protein complex but individually modifies substrate proteins. Its enzymatic activity impacts multiple cellular processes including cell adhesion and immune response.
Pathways
GALNT7 participates significantly in the mucin-type O-glycan biosynthesis pathway. This pathway is essential for generating glycoproteins commonly seen on cell surfaces and in secretions. GALNT7 does not act alone; it works alongside other GalNAc-transferases like GALNT2 which can influence substrate specificity and tissue-specific glycosylation. Another related pathway is the protein O-linked glycosylation pathway where GALNT7 interacts with proteins like MUC1 playing a role in glycoprotein configuration.
GALNT7 has associations with cancers particularly colorectal cancer. Abnormal glycosylation patterns resulting from altered GALNT7 activity can contribute to tumor growth and metastasis. Researchers study GALNT7 expression in cancer tissues to understand its role in oncogenesis. Additionally changes in GALNT7 activity may relate to inflammatory disorders such as Crohn's disease where mucin glycosylation influences intestinal barrier function and inflammation. The interaction between GALNT7 and MUC1 in these contexts is of significant interest especially in examining how it influences disease progression.