|Application ||WB, ICC, E|
|Other Accession||NP_006091, 5174697|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||38214 Da|
|Application Notes||ST3gal6 antibody can be used for detection of ST3gal6 by Western blot at 1 - 2 µg/mL. Antibody can also be used for immunocytochemistry starting at 5 µg/mL.|
|Reconstitution & Storage||ST3gal6 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||ST3gal6 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Involved in the synthesis of sialyl-paragloboside, a precursor of sialyl-Lewis X determinant. Has a alpha-2,3- sialyltransferase activity toward Gal-beta1,4-GlcNAc structure on glycoproteins and glycolipids. Has a restricted substrate specificity, it utilizes Gal-beta1,4-GlcNAc on glycoproteins, and neolactotetraosylceramide and neolactohexaosylceramide, but not lactotetraosylceramide, lactosylceramide or asialo-GM1.|
|Cellular Location||Golgi apparatus membrane; Single-pass type II membrane protein|
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Provided below are standard protocols that you may find useful for product applications.
ST3gal6 Antibody: Sialyltransferases catalyze the transfer of sialic acid from cytidine 5-prime monophospho-N-acetylneuraminic acid (CMP-NeuAc) to terminal positions of glycoprotein and glycolipid carbohydrate groups. Terminal NeuAc residues are key determinants of carbohydrate structures, such as the sialyl-Lewis X determinants, and are widely distributed in many cell types. However, cancer cells often express more heavily sialylated glycans on their cell surface and this feature sometimes correlates with invasiveness. In contrast, expression of ST3gal6, a member of the sialyltransferase family that sialylates type II lactosamine structures on glycoproteins and glycolipids, was found to be significantly decreased by hypermethylation of the gene in gastrointestinal cancer. At least three isoforms of ST3gal6 are known to exist.
Dall’Olio F and Chiricolo M. Sialyltransferases in cancer. Glycoconj. J.2001; 18:841-50.
Okajima T, Fukumoto S, Miyazaki H, et al. Molecular cloning of a novel alpha2,3-sialyltransferase (ST3Gal VI) that sialylates type II lactosamine structures on glycoproteins and glycolipids. J. Biol. Chem.1999; 274:11479-86.
Kawamura YI, Toyota M, Kawashima R, et al. DNA hypermethylation contributes to incomplete synthesis of carbohydrate determinants in gastrointestinal cancer. Gasatroenterology2008; 135:142-51.
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