Serine Palmitoyltransferase (SPTLC2) Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | O15270 |
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Other Accession | NP_004854 |
Clone Names | 3092111 |
Gene ID | 9517 |
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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) |
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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.. |

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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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