|Application ||WB, E|
|Other Accession||P97363, O54694, NP_004854|
|Calculated MW||62924 Da|
|Antigen Region||531-562 aa|
|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||This Serine Palmitoyltransferase (SPTLC2) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 531-562 amino acids from the C-terminal region of human Serine Palmitoyltransferase (SPTLC2).|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|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||Serine Palmitoyltransferase (SPTLC2) Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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.|
|Cellular Location||Endoplasmic reticulum membrane; Single-pass membrane protein|
|Tissue Location||Widely expressed.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent 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.
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.
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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