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SGMS2 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 1
- PROTOCOLS
- BACKGROUND
Application 
| FC, IHC-P, WB, E |
|---|---|
| Primary Accession | Q8NHU3 |
| Other Accession | Q4JM44, Q9D4B1, Q4R763 |
| Reactivity | Human |
| Predicted | Monkey, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 42280 Da |
| Antigen Region | 338-365 aa |
| Gene ID | 166929 |
|---|---|
| Other Names | Phosphatidylcholine:ceramide cholinephosphotransferase 2, Sphingomyelin synthase 2, SGMS2, SMS2 |
| Target/Specificity | This SGMS2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 338-365 amino acids from the C-terminal region of human SGMS2. |
| Dilution | WB~~1:1000 IHC-P~~1:50~100 FC~~1:10~50 |
| 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 | SGMS2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | SGMS2 {ECO:0000303|PubMed:30779713, ECO:0000312|HGNC:HGNC:28395} |
|---|---|
| Function | Sphingomyelin synthase that primarily contributes to sphingomyelin synthesis and homeostasis at the plasma membrane. Catalyzes the reversible transfer of phosphocholine moiety in sphingomyelin biosynthesis: in the forward reaction transfers phosphocholine head group of phosphatidylcholine (PC) on to ceramide (CER) to form ceramide phosphocholine (sphingomyelin, SM) and diacylglycerol (DAG) as by-product, and in the reverse reaction transfers phosphocholine from SM to DAG to form PC and CER. The direction of the reaction appears to depend on the levels of CER and DAG in the plasma membrane (PubMed:14685263, PubMed:17449912, PubMed:17982138, PubMed:18370930). Does not use free phosphorylcholine or CDP-choline as donors (PubMed:14685263). Can also transfer phosphoethanolamine head group of phosphatidylethanolamine (PE) on to ceramide (CER) to form ceramide phosphoethanolamine (CPE) (PubMed:19454763). Regulates receptor-mediated signal transduction via mitogenic DAG and proapoptotic CER, as well as via SM, a structural component of membrane rafts that serve as platforms for signal transduction and protein sorting (PubMed:17449912, PubMed:17982138). To a lesser extent, plays a role in secretory transport via regulation of DAG pool at the Golgi apparatus and its downstream effects on PRKD1 (PubMed:18370930, PubMed:21980337). Required for normal bone matrix mineralization (PubMed:30779713). |
| Cellular Location | Cell membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Note=Primarily localized at the plasma membrane with a small fraction at the Golgi apparatus. |
| Tissue Location | Brain, heart, kidney, liver, muscle and stomach. Also expressed in a number of cell lines such as carcinoma HeLa cells, hepatoma Hep-G2 cells, and colon carcinoma Caco-2 cells |
Provided below are standard protocols that you may find useful for product applications.
Background
Sphingomyelin, a major component of cell and Golgi membranes, is made by the transfer of phosphocholine from phosphatidylcholine onto ceramide, with diacylglycerol as a side product. The protein encoded by this gene is an enzyme that catalyzes this reaction primarily at the cell membrane. The synthesis is reversible, and this enzyme can catalyze the reaction in either direction. The encoded protein is required for cell growth. Three transcript variants encoding the same protein have been found for this gene.
References
Ternes, P., et al. J. Lipid Res. 50(11):2270-2277(2009) Liu, J., et al. Arterioscler. Thromb. Vasc. Biol. 29(6):850-856(2009) Tani, M., et al. Biochem. Biophys. Res. Commun. 381(3):328-332(2009) Wang, W., et al. Plant Cell 20(11):3163-3179(2008) Yeang, C., et al. Biochim. Biophys. Acta 1781(10):610-617(2008) Villani, M., et al. Biochem. J. 414(1):31-41(2008)
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