癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
B3GALTL Antibody
Purified Rabbit Polyclonal Antibody (Pab)
- 产品详情
- 实验流程
- 背景知识
Application 
| WB, IHC |
|---|---|
| Primary Accession | Q6Y288 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | polyclonal |
| Calculated MW | 56564 Da |
| Gene ID | 145173 |
|---|---|
| Other Names | Beta-1, 3-glucosyltransferase, Beta3Glc-T, 241-, Beta-3-glycosyltransferase-like, B3GALTL, B3GTL |
| Dilution | WB~~ 1:1000 IHC~~1:50-100 |
| Format | Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.09% (W/V) sodium azide and 50% glycerol. |
| Storage Conditions | -20℃ |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | B3GLCT (HGNC:20207) |
|---|---|
| Synonyms | B3GALTL, B3GTL |
| Function | Beta-1,3-glucosyltransferase involved in one of the two pathways responsible for protein O-linked fucosylation, a unique post- translational modification of cysteine-knotted proteins that regulates various biological processes. This pathway targets proteins with Thrombospondin type-1 (TSP1) repeats (TSR) in the endoplasmic reticulum. It starts with POFUT2, which attaches fucose via an O- glycosidic bond to a conserved serine or threonine residue. B3GLCT extends this modification by transferring a glucose molecule from UDP- glucose to the fucose. |
| Cellular Location | Endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:16899492}; Single-pass type II membrane protein |
| Tissue Location | Widely expressed, with highest levels in testis and uterus. |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
O-fucosyltransferase that transfers glucose toward fucose with a beta-1,3 linkage. Specifically glucosylates O-linked fucosylglycan on TSP type-1 domains of proteins, thereby contributing to elongation of O-fucosylglycan.
REFERENCES
Heinonen T.Y.K.,et al.Biochem. Biophys. Res. Commun. 309:166-174(2003).
Sato T.,et al.Glycobiology 16:1194-1206(2006).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Dunham A.,et al.Nature 428:522-528(2004).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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