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。
CHST2 Antibody (C-term) 精选
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- 产品详情
- 实验流程
- 背景知识
Application 
| WB, E |
|---|---|
| Primary Accession | Q9Y4C5 |
| Other Accession | Q80WV3, NP_004258.2 |
| Reactivity | Human, Mouse |
| Predicted | Rat, Bovine, Canine, Rabbit, Chicken |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 57857 Da |
| Antigen Region | 493-522 aa |
| Gene ID | 9435 |
|---|---|
| Other Names | Carbohydrate sulfotransferase 2, 282-, Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 2, GST-2, N-acetylglucosamine 6-O-sulfotransferase 1, GlcNAc6ST-1, Gn6ST-1, CHST2, GN6ST |
| Target/Specificity | This CHST2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 493-522 amino acids from the C-terminal region of human CHST2. |
| Dilution | WB~~1:1000 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | CHST2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | CHST2 |
|---|---|
| Synonyms | GN6ST |
| Function | Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues within keratan-like structures on N- and O-linked glycans and within O-linked mucin-type glycans (PubMed:11042394, PubMed:11726653, PubMed:35939855, PubMed:38034954, PubMed:9722682). Selectively transfers the sulfate group onto the terminal GlcNAc of alpha1,3-Man or alpha1,6-Man antenna of complex-type N-glycans depending on glycan composition. Only sulfates terminal GlcNAc of alpha1,3-Man antenna of G0 complex-type N- glycans. Can sulfate keratan-type N-acetyllactosamine (LacNAc) repeats generating epitopes for self versus non-self immune recognition by C- type lectins (PubMed:35939855, PubMed:38034954). Transfers the sulfate group primarily on core 2 GlcNAcbeta1-6(Galbeta1-3)GalNAcalpha-Ser/Thr and with lower efficiency on extended core 1 GlcNAcbeta1-3Galbeta1- 3GalNAcalpha-Ser/Thr based O-linked glycans on peripheral node addressins (PNAds) expressed on the lumenal side of high endothelial venules (HEVs). Shares substrate specificity with CHST4 and both contribute to generate sialyl 6-sulfo Lewis X determinant (also known as MECA-79 epitope) for SELL recognition, a prerequisite for continuous lymphocyte homing into peripheral lymph nodes and antigen immune surveillance (By similarity) (PubMed:9722682). Has no activity toward alpha-linked GlcNAc moiety exposed at the non-reducing ends or to internally located GlcNAc residues (PubMed:11042394). |
| Cellular Location | Golgi apparatus, trans-Golgi network membrane; Single-pass type II membrane protein |
| Tissue Location | Widely expressed. Highly expressed in bone marrow, peripheral blood leukocytes, spleen, brain, spinal cord, ovary and placenta. Expressed by high endothelial cells (HEVs) and leukocytes |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
N-acetylglucosamine-6-O-sulfotransferases, such as CHST2, catalyze the transfer of sulfate from 3-prime-phosphoadenosine 5-prime-phosphosulfate (PAPS) to position 6 of a nonreducing N-acetylglucosamine (GlcNAc) residue (Uchimura et al., 1998 [PubMed 9722682]).
REFERENCES
Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)
Ross, C.J., et al. Nat. Genet. 41(12):1345-1349(2009)
Desko, M.M., et al. Glycobiology 19(10):1068-1077(2009)
Saito, A., et al. J. Hum. Genet. 54(6):317-323(2009)
Kanoh, A., et al. Glycoconj. J. 23 (5-6), 453-460 (2006) :
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