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CHST2 Antibody (Center)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| FC, WB, E |
|---|---|
| Primary Accession | Q9Y4C5 |
| Other Accession | Q80WV3, NP_004258.2 |
| Reactivity | Human |
| Predicted | Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 57857 Da |
| Antigen Region | 309-335 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 309-335 amino acids from the Central region of human CHST2. |
| Dilution | FC~~1:10~50 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 (Center) is for research use only and not for use in diagnostic or therapeutic 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 |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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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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