Recombinant Human Serine Palmitoyltransferase protein is a Human Full Length protein, in the 1 to 562 aa range, expressed in Wheat germ and suitable for ELISA, WB.
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Application | Reactivity | Dilution info | Notes |
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Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases (PubMed:19416851, PubMed:19648650, PubMed:20504773, PubMed:20920666). The SPT complex is composed of SPTLC1, SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer consisting of SPTLC1 and SPTLC2/SPTLC3 forms the catalytic core (PubMed:19416851). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference (PubMed:19416851). 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 (PubMed:19416851, PubMed:19648650). 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 (PubMed:19416851, PubMed:19648650). Crucial for adipogenesis (By similarity).
KIAA0526, LCB2, SPTLC2, Serine palmitoyltransferase 2, Long chain base biosynthesis protein 2, Long chain base biosynthesis protein 2a, Serine-palmitoyl-CoA transferase 2, LCB 2, LCB2a, SPT 2
Recombinant Human Serine Palmitoyltransferase protein is a Human Full Length protein, in the 1 to 562 aa range, expressed in Wheat germ and suitable for ELISA, WB.
pH: 8
Constituents: 0.79% Tris HCl, 0.31% Glutathione
Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases (PubMed:19416851, PubMed:19648650, PubMed:20504773, PubMed:20920666). The SPT complex is composed of SPTLC1, SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer consisting of SPTLC1 and SPTLC2/SPTLC3 forms the catalytic core (PubMed:19416851). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference (PubMed:19416851). 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 (PubMed:19416851, PubMed:19648650). 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 (PubMed:19416851, PubMed:19648650). Crucial for adipogenesis (By similarity).
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
Serine palmitoyltransferase (SPT) sometimes referred to as SPTLC is an enzyme that plays an important role in the initial step of sphingolipid biosynthesis. It catalyzes the condensation of serine and palmitoyl-CoA yielding 3-ketodihydrosphingosine. This enzyme complex consists of subunits SPTLC1 SPTLC2 and sometimes SPTLC3 with a molecular weight around 53 kDa for SPTLC1. Expression of SPT is seen in various tissues including the liver and nervous system supporting its critical functions across the body.
Serine palmitoyltransferase is involved in sphingolipid metabolism contributing to the formation of essential cellular components. It acts as a part of a larger enzyme complex responsible for generating sphingolipid precursors. These sphingolipids play a role in membrane structure and cell signaling affecting processes like cell growth and apoptosis. The enzyme therefore influences fundamental cellular phenomena demonstrating its widespread relevance in biochemistry and cell biology.
Serine palmitoyltransferase is vital in the de novo sphingolipid biosynthesis pathway where it initiates the creation of long-chain bases the core of most sphingolipids. It also links to the lipid metabolism pathway sharing interactions with proteins like ceramide synthase. By producing the starting materials for sphingolipids SPT integrates deeply into lipid regulation and signaling pathways affecting how cells communicate and respond to their environment.
Serine palmitoyltransferase has connections to disorders like hereditary sensory and autonomic neuropathy type I (HSAN1) and metabolic syndromes. Mutations in the SPTLC1 subunit can lead to HSAN1 illustrating its direct involvement in nerve function and health. Additionally altered sphingolipid metabolism implicates SPT in metabolic syndromes where it interacts with proteins like ceramide influencing insulin resistance and lipid homeostasis. These connections emphasize the enzyme's significance in disease development and potential therapeutic targeting.
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ab152996 on a 12.5% SDS-PAGE stained with Coomassie Blue.
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