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500ug
| 产品编号 | bs-16229P |
| 英文名称 | GALNTL6 Antibody Blocking Peptide |
| 中文名称 | GALNTL6蛋白封闭多肽 |
| 英文别名 | EC 2.4.1.41; GalNAc transferase 17; GalNAc-T17; GALNACT20; GALNTL6; GaNTase 17; GLTL6_HUMAN; MGC44629; OTTHUMP00000219021; OTTHUMP00000219023; Polypeptide GalNAc transferase 17; Polypeptide N-acetylgalactosaminyltransferase-like 6; polypeptide N-acetylgalactosaminyltransferase-like 6 UDP-N-acetyl-alpha-D-galactosamine:polypeptideN-acetylgalactosaminyltransferase 20; pp-GaNTase 17; Protein-UDP acetylgalactosaminyltransferase 17; Putative polypeptide N-acetylgalactosaminyltransferase 17; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17; UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-like. |
| 纯化方法 | HPLC |
| 研究领域 | Signal Transduction > Metabolism > Amino Acids Signal Transduction > Protein Trafficking > Golgi Proteins |
| 亚细胞定位 | Golgi apparatus membrane. |
| 相似性 | Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily. Contains 1 ricin B-type lectin domain. |
| 功能 | GalNAc-T17 is a 601 amino acid single-pass type II membrane protein that is a member of the glycosyltransferase 2 family and GalNAc-T subfamily. Localized to the Golgi apparatus and contains a ricin B-type lectin domain, GalNAc-T17 catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GalNAc-T17 contains two conserved domains, an N-terminal domain (domain A, also called GT1 motif), which is likely involved in manganese coordination and substrate binding and a C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is likely involved in catalytic reaction and UDP-Gal binding. GalNAc-T17 exists as two alternatively spliced isoforms and utilizes manganese and calcium as cofactors |
| 保存条件 | Shipped at 4℃. Stored at -20℃ for one year. Avoid repeated freeze/thaw cycles. |
| 注意事项 | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| 背景资料 | GalNAc-T17 is a 601 amino acid single-pass type II membrane protein that is a member of the glycosyltransferase 2 family and GalNAc-T subfamily. Localized to the Golgi apparatus and contains a ricin B-type lectin domain, GalNAc-T17 catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GalNAc-T17 contains two conserved domains, an N-terminal domain (domain A, also called GT1 motif), which is likely involved in manganese coordination and substrate binding and a C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is likely involved in catalytic reaction and UDP-Gal binding. GalNAc-T17 exists as two alternatively spliced isoforms and utilizes manganese and calcium as cofactors. |
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文献和实验or from the literature are missing. In this article, processing parameters for DNA, peptide, antibody, and carbohydrate microarrays are outlined. The applicability of the model experiments is demonstrated and described in detail on the example of short oligonucleotides.
Synthesis and Probing of Membrane-bound Peptide Arrays
the stringency of the blocking conditions and make sure that the primary binding partner and detection reagent (e.g., antibody) are of high purity and are used in the highest possible dilution. Stage
Mapping Protein‐Protein Interactions with Phage‐Displayed Combinatorial Peptide Libraries
. Fack, F., Deroo, S., Kreis, S., and Muller, C.P. 2000. Heteroduplex mobility assay (HMA) pre‐screening: An improved strategy for the rapid identification of inserts selected from phage‐displayed peptide
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