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Serine Palmitoyltransferase (SPTLC2) Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O15270 |
|---|---|
| Other Accession | NP_004854 |
| Clone Names | 3092111 |
| Gene ID | 9517 |
|---|---|
| Other Names | Serine palmitoyltransferase 2, Long chain base biosynthesis protein 2, LCB 2, Long chain base biosynthesis protein 2a, LCB2a, Serine-palmitoyl-CoA transferase 2, SPT 2, SPTLC2, KIAA0526, LCB2 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP2533b was selected from the C-term region of human SPTLC2 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | SPTLC2 (HGNC:11278) |
|---|---|
| Synonyms | KIAA0526, LCB2 |
| Function | Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC2-SPTSSB complex displays a preference for C18-CoA substrate. Plays an important role in de novo sphyngolipid biosynthesis which is crucial for adipogenesis (By similarity). |
| Cellular Location | Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P97363}; Single-pass membrane protein {ECO:0000250|UniProtKB:P97363} |
| Tissue Location | Widely expressed.. |
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
Serine palmitoyltransferase (SPT) is the key enzyme in sphingolipid biosynthesis. It catalyzes the pyridoxal-5-prime-phosphate-dependent condensation of L-serine and palmitoyl-CoA to 3-oxosphinganine.
References
Stachowitz, S., et al., J. Invest. Dermatol. 119(5):1048-1052 (2002).Dias Neto, E., et al., Proc. Natl. Acad. Sci. U.S.A. 97(7):3491-3496 (2000).Weiss, B., et al., Eur. J. Biochem. 249(1):239-247 (1997).Hillier, L.D., et al., Genome Res. 6(9):807-828 (1996).Takeda, J., et al., Hum. Mol. Genet. 2(11):1793-1798 (1993).
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