Recombinant Human Serine Palmitoyltransferase protein (GST tag N-Terminus)
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Recombinant Human Serine Palmitoyltransferase protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 562 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
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
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Serine Palmitoyltransferase protein (GST tag N-Terminus) (AB152996)
ab152996 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
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.
Pathways
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.
Specifications
Form
Liquid
General info
Function
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).
Sequence similarities
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
Target data
Product promise
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