85-1793-96　［取扱停止］GALNTL1, Recombinant, Human, aa27-558 (GALNACT16, GalNAc-T-like protein 1, GALNT16) 20ug　145793

特徴

• O­glycosylation is a ubiquitous post­translational modification present in secreted and membrane­bound proteins. Polypeptide N­acetylgalactosaminyltransferases (GALNTs) catalyze the initial step for O­glycosylation by transferring GalNAc to Thr or Ser residues (GalNAc alpha 1­O­Ser/Thr) in the Golgi compartment. Structurally, the GALNTs consist of an N­terminal catalytic domain tethered by a short linker to a C­terminal ricin­like lectin domain containing three potential carbohydrate­binding sites (1, 2). Twenty distinct GALNT isoforms have been detected in humans. These isoforms display both unique and overlapping substrate specificities (3, 4, 5) with no known universal consensus glycosylation sequence. Glycosylation of mucins results from the successive, often hierarchical, action of several specific GALNTs (6). GALNTL1 is active toward non­glycosylated peptides as well as some glycosylated peptides and is widely expressed in most tissues, especially high in heart, spinal cord and brain (7). Phylogenetically, GALNTL1 is closely related to GALNT2 and GALNT14 (8). The enzymatic activity of recombinant human GALNTL1 was determined using a phosphatase­coupled assay (9).
• Source:Recombinant protein corresponding to Asp27-Thr558 from human GALNTL1, fused to 6-his tag at C-terminal, NS0-derived.
• Molecular Weight:~55-61kD
• Endotoxin:<1.0EU/1ug (LAL method)
• Storage and Stability:May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.