Custom Services order now ship next day

Lipid / Cholesterol Metabolism

Representative Targets in Lipid / Cholesterol Metabolism Full List of Targets in Lipid / Cholesterol Metabolism Tested Data-Supported Products for Targeting Lipid / Cholesterol Metabolism

Lipid metabolism encompasses the complex biochemical processes involved in the synthesis, breakdown, and utilization of lipids, including fats, oils, and cholesterol. These processes are crucial for maintaining energy balance, cellular structure, and signaling within the body. Lipid metabolism can be broadly divided into catabolic processes, which break down lipids to produce energy, and anabolic processes, which involve the synthesis of lipids for various biological functions. The catabolism of triglycerides, the most common type of body fat, occurs in the adipose tissue through lipolysis, releasing free fatty acids and glycerol into the bloodstream. These fatty acids can then be oxidized within the mitochondria of cells in a process known as β-oxidation to generate acetyl-CoA, which enters the citric acid cycle to produce ATP, NADH, and FADH2, which are key energy molecules. Conversely, the anabolic side of lipid metabolism involves the synthesis of fatty acids, which occurs primarily in the liver and, to a lesser extent, in adipose tissue. This process, driven by enzymes such as acetyl-CoA carboxylase and fatty acid synthase, converts acetyl-CoA into fatty acids, which can then be esterified to glycerol to form triglycerides for storage or transported to other tissues.

Figure 1 Overview of Lipid Metabolism. (Ward, 2021) Figure 1 Overview of Lipid Metabolism. (Ward, 2021)

Cholesterol is synthesized in a complex multi-step enzymatic process starting from acetyl-CoA, primarily within the cytoplasm and endoplasmic reticulum of liver cells. The rate-limiting step in cholesterol synthesis is catalyzed by the enzyme HMG-CoA reductase, which converts HMG-CoA to mevalonate. This enzyme is a primary target for statin drugs, widely used to lower blood cholesterol levels. Once synthesized, cholesterol is either stored in the liver or transported to peripheral tissues through various lipoproteins, such as LDL (low-density lipoprotein) and HDL (high-density lipoprotein), which are key players in cholesterol transport and metabolism. LDL is often termed "bad" cholesterol because it transports cholesterol to the tissues and can deposit it in artery walls, leading to atherosclerosis. Conversely, HDL is known as "good" cholesterol due to its role in transporting cholesterol away from the arteries and back to the liver for excretion or recycling. The regulation of cholesterol metabolism is finely tuned by dietary intake, cellular cholesterol levels, and hormonal signals, primarily through feedback inhibition mechanisms involving the suppression of HMG-CoA reductase activity. Additionally, excess cholesterol can be converted into bile acids in the liver, facilitating its elimination from the body. This conversion is another regulatory mechanism that maintains cholesterol homeostasis and aids in dietary fat digestion.

Figure 2 Schematic representation of the cellular cholesterol metabolism. (Cardoso, 2021)Figure 2 Schematic representation of the cellular cholesterol metabolism. (Cardoso, 2021)

Representative Targets in Lipid / Cholesterol Metabolism


AMACR, or Alpha-Methylacyl-CoA Racemase, is an enzyme that plays a crucial role in the metabolism of branched-chain fatty acids and bile acid intermediates. It is involved in the conversion of (R)-stereoisomers to (S)-stereoisomers in the mitochondria and peroxisomes, a necessary step in the degradation of certain fatty acids, particularly those with methyl branches. This conversion is essential for the proper catabolism of these fatty acids, which otherwise could accumulate and lead to toxic effects. AMACR is expressed in a variety of tissues, including liver, kidney, and prostate, indicating its widespread importance in fatty acid metabolism across different physiological systems. The enzyme's activity is particularly significant in the metabolism of dietary cholesterol and the synthesis of bile acids, which are critical for the digestion and absorption of fats. AMACR is highly overexpressed in prostate cancer cells compared to normal prostate tissue, making it a valuable diagnostic and prognostic marker of prostate cancer.

Recommended Mouse Anti-AMACR mAb (CAT#: HPAB-0570-YJ)
Figure 3 Mouse Anti-AMACR Recombinant Antibody (clone 4A12) in IF
Figure 3 Immunofluorescence analysis of Rat-brain tissue. 1.AMACR Monoclonal Antibody (red) was diluted at 1:200 (4°C, overnight). 2, Cy3 labled Secondary Antibody was diluted at 1:300 (room temperature, 50min).3, Picture B: DAPI(blue) 10min. Picture A:Target. Picture B: DAPI. Picture C:merge of A+B.
Recommended Mouse Anti-AMACR mAb (CAT#: ZG-0283F)
Figure 4 Mouse Anti-AMACR Recombinant Antibody (ZG-0283F) in IHC
Figure 4 Immunohistochemical analysis of paraffin-embedded human normal prostate tissue (left) and prostate adenocarcinoma tissue (right), showing the cytoplasmic localization of DAB staining with AMACR monoclonal antibody.
Recommended Mouse Anti-AMACR mAb (CAT#: ZG-0025J)
Figure 5 Mouse Anti-AMACR Recombinant Antibody (ZG-0025J) in IHC
Figure 5 Immunohistochemical analysis of paraffin-embedded Prostatic carcinoma. 1. Antibody was diluted at 1:200 (4°C overnight). 2, TRIS-EDTA of pH8.0 was used for antigen retrieval. 3, Secondary Antibody was diluted at 1:200 (room temperature, 30min).


FASN, or Fatty Acid Synthase, is a multifunctional enzyme complex essential in the biosynthesis of long-chain fatty acids, notably palmitate, from acetyl-CoA and malonyl-CoA, using NADPH as a cofactor. This enzyme predominantly operates in liver and adipose tissues, where it plays a pivotal role in converting excess carbohydrates into fatty acids, subsequently stored as triglycerides. FASN's functionality is not limited to lipid metabolism; it significantly impacts cell signaling and protein modification, which influences membrane composition and protein function across cellular systems. Regulated tightly by both nutritional and hormonal signals, FASN's activity reflects the body's metabolic state and adaptation to varying energy demands. Importantly, FASN is consistently overexpressed in many types of cancer, supporting the proliferation of tumor cells by meeting their increased demands for membrane lipid synthesis, thus contributing to enhanced growth and survival. Consequently, FASN has been identified as a potential oncogenic driver and a viable target for anticancer therapies. Inhibitors targeting FASN are being explored to exploit cancer cells' dependence on de novo fatty acid synthesis for their progression and survival. Beyond cancer, aberrant FASN activity is linked to various metabolic disorders, marking it as a critical enzyme in metabolic regulation and a potential focal point for therapeutic interventions in metabolic syndromes as well as cancer treatment.

Recommended Mouse Anti-FASN mAb (CAT#: ZG-0335J)
 Figure 6 Mouse Anti-FASN Recombinant Antibody (ZG-0335J) in ICC
Figure 6 Mouse Anti-FASN Recombinant Antibody (ZG-0335J) in ICC. Immunocytochemistry staining of Hela cells fixed with 4% Paraformaldehyde and using anti-Fatty Acid Synthase mouse mAb (dilution 1:200).
Recommended Mouse Anti-FASN mAb (CAT#: ZG-0336J)
Figure 7 Rabbit Anti-FASN Antibody (ZG-0665J) in FC
Figure 7 Mouse Anti-FASN Recombinant Antibody (ZG-0336J) in IP. Immunoprecipitation analysis of CHO-K1 cell lysates using Fatty Acid Synthase mouse mAb.
Recommended Rabbit Anti-FASN mAb (CAT#: ZG-0665J)
 Figure 8 Rabbit Anti-FASN Antibody (ZG-0665J) in FC
Figure 8 Rabbit Anti-FASN Antibody (ZG-0665J) in FC. Overlay histogram showing A549 cells stained with this product (red line) at 1:50. The cells were fixed with 70% Ethylalcohol (18h) and then incubated in 10% normal goat serum to block non-specific protein-protein interactions followedby the antibody (1µg/1*106cells) for 1 h at 4°C. The secondary antibody used was FITC-conjugated goat anti-rabbit IgG (H+L) at 1/200 dilution for 30min at 4°C. Control antibody (green line) was Rabbit IgG (1µg/1*106cells) used under the same conditions. Acquisition of>10,000 events was performed.


PLA2G7, also known as Platelet-Activating Factor Acetylhydrolase (PAF-AH) or Lipoprotein-associated phospholipase A2 (Lp-PLA2), is an enzyme that hydrolyzes the sn-2 acetyl group from platelet-activating factor (PAF), a potent phospholipid activator and mediator involved in a range of biological processes, including inflammation, allergy, and thrombosis. PAF-AH thereby serves as a regulatory enzyme in the PAF pathway, modulating the levels of this bioactive lipid to maintain physiological balance and mitigate excessive inflammatory responses. Predominantly associated with low-density lipoproteins (LDL) in the bloodstream, PLA2G7 is involved in the pathogenesis of atherosclerosis. It hydrolyzes oxidized phospholipids in LDL, potentially reducing the pro-inflammatory properties of oxidized LDL, a key factor in the development of atherosclerotic plaques. Due to its role in cardiovascular disease, PLA2G7 has attracted interest as a biomarker for cardiovascular risk assessment and as a therapeutic target. Elevated levels of Lp-PLA2 are associated with an increased risk of coronary artery disease, stroke, and myocardial infarction.In addition to cardiovascular implications, the activity of PLA2G7 is linked to other inflammatory diseases such as asthma and rheumatoid arthritis. By regulating the levels of inflammatory mediators, PLA2G7 potentially influences the severity and progression of inflammatory conditions.

Recommended Rabbit Anti-PLA2G7 mAb (CAT#: VS3-FY627)
Figure 9 Mouse Anti-PLA2G7 Antibody (ZG-0157U) in WB
Figure 9 Mouse Anti-PLA2G7 Antibody (ZG-0157U) in WB. All lanes: Mouse anti-human Platelet-activati ng factor acetylhydrolase monoclonal Antibody at 1μg/ml. Lane 1: mouse spleen tissue. Secondary: HRP labeled Goat polyclonal to Mouse IgG at 1/3000 dilution. Predicted band size : 48kd. Observed band size : 48kd. Additional bands at: 85kd.

Full List of Targets in Lipid / Cholesterol Metabolism

Biomarker Alternative Names Gene ID UniProt ID Roles
ACACA Acetyl-CoA Carboxylase Alpha; Acetyl-Coenzyme A Carboxylase Alpha; Acetyl-CoA Carboxylase 1; ACC-Alpha; ACAC; ACC1 31 Q13085 Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. There are two ACC forms, alpha and beta, encoded by two different genes. ACC-alpha is highly enriched in lipogenic tissues. The enzyme is under long term control at the transcriptional and translational levels and under short term regulation by the phosphorylation/dephosphorylation of targeted serine residues and by allosteric transformation by citrate or palmitoyl-CoA. Multiple alternatively spliced transcript variants divergent in the 5' sequence and encoding distinct isoforms have been found for this gene.
ACACB Acetyl-CoA Carboxylase Beta; Acetyl-Coenzyme A Carboxylase Beta; Acetyl-CoA Carboxylase 2; ACC-Beta; ACC2; ACCB; EC; HACC275 32 O00763 Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. ACC-beta is thought to control fatty acid oxidation by means of the ability of malonyl-CoA to inhibit carnitine-palmitoyl-CoA transferase I, the rate-limiting step in fatty acid uptake and oxidation by mitochondria. ACC-beta may be involved in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. There is evidence for the presence of two ACC-beta isoforms.
ACLY ATP Citrate Lyase; ATP-Citrate (Pro-S-)-Lyase; Citrate Cleavage Enzyme; EC; ACL; ATP Citrate Synthase; ATP-Citrate Synthase; ATPCL; CLATP; 47 A0A024R1T9 ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently identical subunits. It catalyzes the formation of acetyl-CoA and oxaloacetate from citrate and CoA with a concomitant hydrolysis of ATP to ADP and phosphate. The product, acetyl-CoA, serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis. In nervous tissue, ATP citrate-lyase may be involved in the biosynthesis of acetylcholine. Multiple transcript variants encoding distinct isoforms have been identified for this gene.
ALOX5 Arachidonate 5-Lipoxygenase; EC; 5-LO; LOG5; Arachidonic 5-Lipoxygenase Delta-10-13 Isoform; Arachidonic 5-Lipoxygenase Delta-P10 Isoform; Arachidonic 5-Lipoxygenase Alpha-10 Isoform; Arachidonic 5-Lipoxygenase Delta-13 Isoform; 240 P09917 This gene encodes a member of the lipoxygenase gene family and plays a dual role in the synthesis of leukotrienes from arachidonic acid. The encoded protein, which is expressed specifically in bone marrow-derived cells, catalyzes the conversion of arachidonic acid to 5(S)-hydroperoxy-6-trans-8,11,14-cis-eicosatetraenoic acid, and further to the allylic epoxide 5(S)-trans-7,9-trans-11,14-cis-eicosatetrenoic acid (leukotriene A4). Leukotrienes are important mediators of a number of inflammatory and allergic conditions. Mutations in the promoter region of this gene lead to a diminished response to antileukotriene drugs used in the treatment of asthma and may also be associated with atherosclerosis and several cancers. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2012]
AMACR Alpha-Methylacyl-CoA Racemase; 2-Methylacyl-CoA Racemase; EC; AMACRD; CBAS4; P504S; RACE; RM; 23600 Q9UHK6 This gene encodes a racemase. The encoded enzyme interconverts pristanoyl-CoA and C27-bile acylCoAs between their (R)- and (S)-stereoisomers. The conversion to the (S)-stereoisomers is necessary for degradation of these substrates by peroxisomal beta-oxidation. Encoded proteins from this locus localize to both mitochondria and peroxisomes. Mutations in this gene may be associated with adult-onset sensorimotor neuropathy, pigmentary retinopathy, and adrenomyeloneuropathy due to defects in bile acid synthesis. Alternatively spliced transcript variants have been described. Read-through transcription also exists between this gene and the upstream neighboring C1QTNF3 (C1q and tumor necrosis factor related protein 3) gene.
ASAH2 HNAC1; BCDase; LCDase; NCDase; N-Cdase 56624 Q9NR71 Ceramidases (EC, such as ASAH2, catalyze hydrolysis of the N-acyl linkage of ceramide, a second messenger in a variety of cellular events, to produce sphingosine. Sphingosine exerts both mitogenic and apoptosis-inducing activities, and its phosphorylated form functions as an intra- and intercellular second messenger (see MIM 603730).
CHKB CHKB; CHETK; Choline/Ethanolamine Kinase; CKEKB; EK; Choline/Ethanolamine Kinase Beta; EC; EKB; Choline Kinase-Like Protein; EC; CKB; CK; CHKL; MDCMC; Choline Kinase Beta 1120 Q9Y259 Choline kinase (CK) and ethanolamine kinase (EK) catalyze the phosphorylation of choline/ethanolamine to phosphocholine/phosphoethanolamine. This is the first enzyme in the biosynthesis of phosphatidylcholine/phosphatidylethanolamine in all animal cells. The highly purified CKs from mammalian sources and their recombinant gene products have been shown to have EK activity also, indicating that both activities reside on the same protein. The choline kinase-like protein encoded by CHKL belongs to the choline/ethanolamine kinase family; however, its exact function is not known. Read-through transcripts are expressed from this locus that include exons from the downstream CPT1B locus.
ENPP2 ENPP2; ectonucleotide pyrophosphatase/phosphodiesterase 2; ATX; NPP2; ATX-X; PDNP2; LysoPLD; AUTOTAXIN; PD-IALPH 5168 Q13822 The protein encoded by this gene functions as both a phosphodiesterase, which cleaves phosphodiester bonds at the 5' end of oligonucleotides, and a phospholipase, which catalyzes production of lysophosphatidic acid (LPA) in extracellular fluids. LPA evokes growth factor-like responses including stimulation of cell proliferation and chemotaxis. This gene product stimulates the motility of tumor cells and has angiogenic properties, and its expression is upregulated in several kinds of carcinomas. The gene product is secreted and further processed to make the biologically active form. Several alternatively spliced transcript variants encoding different isoforms have been identified.
ENPP7 Ectonucleotide Pyrophosphatase/Phosphodiesterase 7; Alkaline Sphingomyelin Phosphodiesterase; Intestinal Alkaline Sphingomyelinase; Alkaline Sphingomyelinase; ALK-Smase; E-NPP 7; NPP-7; EC; NPP7 339221 Q6UWV6 ENPP7 (Ectonucleotide Pyrophosphatase/Phosphodiesterase 7) is a Protein Coding gene. Diseases associated with ENPP7 include colorectal cancer. Among its related pathways are Metabolism and Sphingolipid metabolism. GO annotations related to this gene include sphingomyelin phosphodiesterase activity. An important paralog of this gene is ENPP3.
FASN FAS; OA-519; SDR27X1 2194 P49327 The enzyme encoded by this gene is a multifunctional protein. Its main function is to catalyze the synthesis of palmitate from acetyl-CoA and malonyl-CoA, in the presence of NADPH, into long-chain saturated fatty acids. In some cancer cell lines, this protein has been found to be fused with estrogen receptor-alpha (ER-alpha), in which the N-terminus of FAS is fused in-frame with the C-terminus of ER-alpha.
GPLD1 GPLD1; PLD; GPI-Specific Phospholipase D; Glycosyl-Phosphatidylinositol-Specific Phospholipase D; Phosphatidylinositol-Glycan-Specific Phospholipase D; Glycoprotein Phospholipase D; GPIPLDM; EC; PI-G PLD; GPI-PLD 2822 P80108 Many proteins are tethered to the extracellular face of eukaryotic plasma membranes by a glycosylphosphatidylinositol (GPI) anchor. The GPI-anchor is a glycolipid found on many blood cells. The protein encoded by this gene is a GPI degrading enzyme. Glycosylphosphatidylinositol specific phospholipase D1 hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans, thereby releasing the attached protein from the plasma membrane.
HMGCR 3-Hydroxy-3-Methylglutaryl-CoA Reductase; 3-Hydroxy-3-Methylglutaryl CoA Reductase (NADPH); 3-Hydroxy-3-Methylglutaryl-Coenzyme A Reductase; Hydroxymethylglutaryl-CoA Reductase; HMG-CoA Reductase; EC; EC 1.1.1; LDLCQ3 3156 P04035 HMG-CoA reductase is the rate-limiting enzyme for cholesterol synthesis and is regulated via a negative feedback mechanism mediated by sterols and non-sterol metabolites derived from mevalonate, the product of the reaction catalyzed by reductase. Normally in mammalian cells this enzyme is suppressed by cholesterol derived from the internalization and degradation of low density lipoprotein (LDL) via the LDL receptor. Competitive inhibitors of the reductase induce the expression of LDL receptors in the liver, which in turn increases the catabolism of plasma LDL and lowers the plasma concentration of cholesterol, an important determinant of atherosclerosis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2008]
LIPE HSL; LHS; REH; AOMS4; FPLD6 3991 Q05469 The protein encoded by this gene has a long and a short form, generated by use of alternative translational start codons. The long form is expressed in steroidogenic tissues such as testis, where it converts cholesteryl esters to free cholesterol for steroid hormone production. The short form is expressed in adipose tissue, among others, where it hydrolyzes stored triglycerides to free fatty acids.
LPL LIPD; HDLCQ11 4023 P06858 LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. LPL functions as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake.
MGLL MGL; HUK5; MAGL; HU-K5 11343 Q99685 This gene encodes a serine hydrolase of the AB hydrolase superfamily that catalyzes the conversion of monoacylglycerides to free fatty acids and glycerol. The encoded protein plays a critical role in several physiological processes including pain and nociperception through hydrolysis of the endocannabinoid 2-arachidonoylglycerol. Expression of this gene may play a role in cancer tumorigenesis and metastasis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
NAAA NAAA; Human NAAA 27163 Q02083
PLA2G1B P; sP; Pla2a; sPLA2IB; phospholipase A2; PLA2-Ib; group IB phospholipase A2; phosphatidylcholine 2-acylhydrolase 1B 5319 P04054 This gene encodes a secreted member of the phospholipase A2 (PLA2) class of enzymes, which is produced by the pancreatic acinar cells. The encoded calcium-dependent enzyme catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to release arachidonic acid (AA) and lysophospholipids. AA is subsequently converted by downstream metabolic enzymes to several bioactive lipophilic compounds (eicosanoids), including prostaglandins (PGs) and leukotrienes (LTs). The enzyme may be involved in several physiological processes including cell contraction, cell proliferation and pathological response.
PLA2G2A MOM1; PLA2; PLA2B; PLA2L; PLA2S; PLAS1; sPLA2 5320 P14555 This gene product belongs to group II, which contains secreted form of PLA2, an extracellular enzyme that has a low molecular mass and requires calcium ions for catalysis.
PLA2G4A PLA2G4A; PLA2G4; CPLA2-Alpha; Phosphatidylcholine 2-Acylhydrolase; Cytosolic Phospholipase A2; Phospholipase A2, Group IVA (Cytosolic, Calcium-Dependent); Lysophospholipase; Phospholipase A2 Group IVA; CPLA2 5321 P47712 Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response
PLA2G7 PAFAD; PAFAH; LP-PLA2; LDL-PLA2 7941 Q13093 In the blood Lp-PLA2 travels mainly with low-density lipoprotein (LDL). Less than 20% is associated with high-density lipoprotein HDL. Several lines of evidence suggest that HDL-associated Lp-PLA2 may substantially contribute to the HDL antiatherogenic activities.
PLD1 5337 Q13393 This gene encodes a phosphatidylcholine-specific phospholipase which catalyzes the hydrolysis of phosphatidylcholine in order to yield phosphatidic acid and choline. The enzyme may play a role in signal transduction and subcellular trafficking. Alternative splicing results in multiple transcript variants with both catalytic and regulatory properties.
PNPLA2 ATGL; Desnutrin; plpl; plpl2; Pnpla2; TTS 2.2; TTS2; TTS2.2; ZETA 57104 Q96AD5 Adipose triglyceride lipase, also known as patatin-like phospholipase domain-containing protein 2 and ATGL, is an enzyme that in humans is encoded by the PNPLA2 gene.
PTGDS PDS; PGD2; PGDS; LPGDS; PGDS2; L-PGDS; prostaglandin D2 synthase; prostaglandin-H2 D-isomerase; PGD2 synthase; beta-trace protein; cerebrin-28; glutathione-independent PGD synthase; glutathione-independent PGD synthetase; prostaglandin D synthase; prostaglandin D2 synthase 21kDa (brain); testis tissue sperm-binding protein Li 63n 5730 A0A024R8G3 PTGDS is a glutathione-independent prostaglandin D synthase that catalyzes the conversion of prostaglandin H2 (PGH2) to postaglandin D2 (PGD2). PGD2 functions as a neuromodulator as well as a trophic factor in the central nervous system. PGD2 is also involved in smooth muscle contraction/relaxation and is a potent inhibitor of platelet aggregation. This gene is preferentially expressed in brain.
PTGES2 PTGES2; prostaglandin E synthase 2; C9orf15,chromosome 9 open reading frame 15; FLJ14038; C9orf15; FLJ14038; Gamma interferon activated transcriptional element binding factor 1; GATE binding factor 1; GBF1; Membrane associated prostaglandin E synthase 2; MGC11289; Microsomal prostaglandin E synthase 2; mPGES 2; mPGES-2; PGES2; PGES2_HUMAN; Prostaglandin E synthase 2; Prostaglandin E synthase 2 truncated form; PTGES 2; PTGES2; OTTHUMP00000022231; OTTHUMP00000022232; OTTHUMP00000215363; GATE-binding factor 1; microsomal prostaglandin E synthase 2; microsomal prostaglandin E synthase-2; membrane-associated prostaglandin E synthase 2; gamma-interferon-activated; GBF1; PGES2; C9orf15; mPGES-2; 80142 Q9H7Z7 The protein encoded by this gene is a membrane-associated prostaglandin E synthase, which catalyzes the conversion of prostaglandin H2 to prostaglandin E2. This protein also has been shown to activate the transcription regulated by a gamma-interferon-activated transcription element (GATE). Multiple transcript variants have been found for this gene. [provided by RefSeq, Jun 2009]
PTGES3 PTGES3; P23; TEBP; Prostaglandin E synthase 3; Cytosolic prostaglandin E2 synthase; cPGES; Hsp90 co-chaperone; Progesterone receptor complex p23; Telomerase-binding protein p23 10728 Q15185 The protein encoded by this gene is also known as p23 which functions as a chaperone which is required for proper functioning of the glucocorticoid and other steroid receptors.
PTGIS PTGIS; Prostaglandin I2 (Prostacyclin) Synthase; Prostacyclin Synthase; PGIS; Prostaglandin I2 Synthase; EC; Cytochrome P450, Family 8, Subfamily A, Polypeptide 1; CYP8A1; PTGI; Subfamily A; Polypeptide 1; Family 8 5740 Q16647 This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. However, this protein is considered a member of the cytochrome P450 superfamily on the basis of sequence similarity rather than functional similarity. This endoplasmic reticulum membrane protein catalyzes the conversion of prostglandin H2 to prostacyclin (prostaglandin I2), a potent vasodilator and inhibitor of platelet aggregation. An imbalance of prostacyclin and its physiological antagonist thromboxane A2 contribute to the development of myocardial infarction, stroke, and atherosclerosis.
SMPD1 SMPD1; Sphingomyelin Phosphodiesterase 1, Acid Lysosomal; Acid Sphingomyelinase; ASMASE; Sphingomyelin Phosphodiesterase; NPD; ASM 6609 P17405 The protein encoded by this gene is a lysosomal acid sphingomyelinase that converts sphingomyelin to ceramide. The encoded protein also has phospholipase C activity. Defects in this gene are a cause of Niemann-Pick disease type A (NPA) and Niemann-Pick disease type B (NPB). Multiple transcript variants encoding different isoforms have been identified.
SMPD3 SMPD3; Sphingomyelin Phosphodiesterase 3; Sphingomyelin Phosphodiesterase 3, Neutral Membrane (Neutral Sphingomyelinase II); Neutral Sphingomyelinase II; NSMASE2; EC 55512 Q9NY59 Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization.
SOAT1 SOAT1; ACACT1; Sterol O-Acyltransferase 1; ACACT; ACAT-1; Acyl-Coenzyme A:Cholesterol Acyltransferase 1; ACAT1; Cholesterol Acyltransferase 1; Sterol O-Acyltransferase (Acyl-Coenzyme A: Cholesterol Acyltransferase) 1; SOAT; STAT; ACAT 6646 P35610 The protein encoded by this gene belongs to the acyltransferase family. It is located in the endoplasmic reticulum, and catalyzes the formation of fatty acid-cholesterol esters. This gene has been implicated in the formation of beta-amyloid and atherosclerotic plaques by controlling the equilibrium between free cholesterol and cytoplasmic cholesteryl esters. Alternatively spliced transcript variants have been found for this gene.
SPHK1 Sphingosine Kinase 1; SPK 1; SK 1; SPHK; EC; SPK 8877 Q9NYA1 The protein encoded by this gene catalyzes the phosphorylation of sphingosine to form sphingosine-1-phosphate (S1P), a lipid mediator with both intra- and extracellular functions. Intracellularly, S1P regulates proliferation and survival, and extracellularly, it is a ligand for cell surface G protein-coupled receptors. This protein, and its product S1P, play a key role in TNF-alpha signaling and the NF-kappa-B activation pathway important in inflammatory, antiapoptotic, and immune processes. Phosphorylation of this protein alters its catalytic activity and promotes its translocation to the plasma membrane. Alternative splicing results in multiple transcript variants encoding different isoforms.

Tested Data-Supported Products for Targeting Lipid / Cholesterol Metabolism

  1. Ward, Ashley V., Steven M. Anderson, and Carol A. Sartorius. "Advances in analyzing the breast cancer lipidome and its relevance to disease progression and treatment." Journal of mammary gland biology and neoplasia 26.4 (2021): 399-417.
  2. Cardoso, Diana, and Esperanza Perucha. "Cholesterol metabolism: a new molecular switch to control inflammation." Clinical Science 135.11 (2021): 1389-1408.

For research use only. Not intended for any clinical use.

Send Inquiry

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

  • 0
  • 0
    Go to compare

    Go to compare