|Other Names||CMP-N-acetylneuraminate-poly-alpha-2, 8-sialyltransferase, 2499-, Alpha-2, 8-sialyltransferase 8D, Polysialyltransferase-1, Sialyltransferase 8D, SIAT8-D, Sialyltransferase St8Sia IV, ST8SiaIV, ST8SIA4, PST, PST1, SIAT8D|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||PST, PST1, SIAT8D|
|Function||Catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid (PSA), which is present on the embryonic neural cell adhesion molecule (N-CAM), necessary for plasticity of neural cells.|
|Cellular Location||Golgi apparatus membrane; Single-pass type II membrane protein|
|Tissue Location||Highly expressed in fetal brain, lung and kidney and in adult heart, spleen and thymus. Present to a lesser extent in adult brain, placenta, lung, large and small intestine and peripheral blood leukocytes|
email@example.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
The protein encoded by this gene catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). The encoded protein, which is a member of glycosyltransferase family 29, is a type II membrane protein that may be present in the Golgi apparatus.
Johnson, M.P., et al. Hum. Genet. 126(5):655-666(2009)Foley, D.A., et al. J. Biol. Chem. 284(23):15505-15516(2009)Otowa, T., et al. J. Hum. Genet. 54(2):122-126(2009)Sonuga-Barke, E.J., et al. Am. J. Med. Genet. B Neuropsychiatr. Genet. 147B (8), 1359-1368 (2008) :Schreiber, S.C., et al. Gastroenterology 134(5):1555-1566(2008)Close, B.E., et al. Glycobiology 11(11):997-1008(2001)Angata, K., et al. J. Biol. Chem. 276(18):15369-15377(2001)
If you have any additional inquiries please email technical services at firstname.lastname@example.org.