|Application ||WB, E|
|Calculated MW||52744 Da|
|Antigen Region||26-57 aa|
|Other Names||Serine palmitoyltransferase 1, Long chain base biosynthesis protein 1, LCB 1, Serine-palmitoyl-CoA transferase 1, SPT 1, SPT1, SPTLC1, LCB1|
|Target/Specificity||This SPTLC1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 26-57 amino acids from the N-terminal region of human SPTLC1.|
|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||SPTLC1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 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-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1- SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference.|
|Cellular Location||Endoplasmic reticulum membrane; Single-pass membrane protein|
|Tissue Location||Widely expressed. Not detected in small intestine.|
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).
Nicholson, G.A., et al., Am. J. Hum. Genet. 69(3):655-659 (2001).
Dawkins, J.L., et al., Nat. Genet. 27(3):309-312 (2001).
Bejaoui, K., et al., Nat. Genet. 27(3):261-262 (2001).
Perry, D.K., et al., J. Biol. Chem. 275(12):9078-9084 (2000).
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