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- bs-16227P
- 2025年10月16日
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500ug
| 产品编号 | bs-16227P |
| 英文名称 | GALNTL4 Antibody Blocking Peptide |
| 中文名称 | GALNTL4蛋白封闭多肽 |
| 英文别名 | GalNAc T like protein 4; GalNAc T15; GLT18_HUMAN; GalNAc transferase 18; GALNT15; GALNT18; N acetylgalactosaminyltransferase 15 UDP N acetyl alpha D galactosamine:polypeptide; N acetylgalactosaminyltransferase like 4; N acetylgalactosaminyltransferase like protein 4 UDP N acetyl alpha D galactosamine:polypeptide; Polypeptide GalNAc transferase like protein 4; pp GaNTase like protein 4; Protein UDP acetylgalactosaminyltransferase like protein 4; Protein UDP acetylgalactosaminyltransferase like protein 4 UDP GalNAc:polypeptide; Putative polypeptide N acetylgalactosaminyltransferase like protein 4; UDP GalNAc:polypeptide N acetylgalactosaminyltransferase like protein 4. |
| 纯化方法 | HPLC |
| 亚细胞定位 | Golgi Apparatus membrane; Single-pass type II membrane protein |
| 相似性 | Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily. Contains 1 ricin B-type lectin domain. |
| 功能 | GALNTL4 may catalyze 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. |
| 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 | The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosaminyl) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in Golgi apparatus. GalNAc-TL4, also known as LGALS14 or polypeptide GalNAc transferase-like protein 4, is a 607 amino acid single-pass type II membrane protein belonging to the glycosyltransferase 2 family and GalNAc-T subfamily. Localizing to Golgi apparatus, GalNAc-TL4 utilizes manganese and calcium as cofactors and may assist with the transfer of N-acetyl-D-galactosamine to a serine or threonine residue on protein receptors. GalNAc-TL4 likely catalyzes the initial reaction in O-linked oligosaccharide biosynthesis and contains a ricin B-type lectin domain, which binds to GalNAc and contributes to glycopeptide specificity, and two conserved domains located in the glycosyltransferase region. The N-terminal domain, also known as domain A or GT1 motif, may be involved in manganese coordination and substrate binding while the C-terminal domain, also known as domain B or Gal/GalNAc-T motif, is likely involved in catalytic reaction and UDP-Gal binding. GalNAc-TL4 exists as two alternatively spliced isoforms. |
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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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