CEL Mouse
Bile salt-activated lipase, BAL, EC 3.1.1.13, EC 3.1.1.3, Bile salt-stimulated lipase, BSSL, Bucelipase, Carboxyl ester lipase, Cholesterol esterase, Pancreatic lysophospholipase, Sterol esterase, CEL, FAP, BSDL, CELL, FAPP, LIPA, Cease, MODY8.
Description
CEL Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 585 amino acids (21-599 aa) and having a molecular mass of 64.5kDa.
CEL is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
Carboxyl ester lipase (CEL), previously known as cholesterol esterase or bile salt-stimulated lipase, is an enzyme that breaks down fats (lipolytic enzyme). It can hydrolyze various lipids, including cholesteryl esters, phospholipids, triglycerides, diglycerides, monoglycerides, ceramides, and lysophospholipids. The enzyme's activity is regulated by its carboxyl terminus, which interacts with a surface loop to partially block the active site. The active site, consisting of serine, histidine, and aspartate, is located in the center of the enzyme and is partially covered by this loop. When bile salts bind to the loop domain, the active site becomes accessible to water-insoluble substrates. CEL is primarily produced in the pancreas and lactating mammary gland but is also found in the liver, macrophages, and blood vessel walls.
Recombinant Mouse CEL was expressed in Sf9 insect cells using a Baculovirus expression system. It is a single, glycosylated polypeptide chain containing 585 amino acids (21-599 aa), resulting in a molecular mass of 64.5 kDa. A 6-amino acid His-tag is fused to the C-terminus for purification purposes. The protein is purified using proprietary chromatographic techniques.
The CEL solution is provided at a concentration of 0.5 mg/ml in a buffer containing 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
For short-term storage (2-4 weeks), store the CEL solution at 4°C. For extended storage, freeze the solution at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for long-term storage. Avoid repeated freeze-thaw cycles to maintain protein stability.
The specific activity of CEL is greater than 100,000 pmol/min/µg. This is determined by measuring the amount of enzyme required to hydrolyze 1.0 µmole of p-nitrophenyl butyrate to p-nitrophenol per minute at pH 7.5 and 25°C.
Bile salt-activated lipase, BAL, EC 3.1.1.13, EC 3.1.1.3, Bile salt-stimulated lipase, BSSL, Bucelipase, Carboxyl ester lipase, Cholesterol esterase, Pancreatic lysophospholipase, Sterol esterase, CEL, FAP, BSDL, CELL, FAPP, LIPA, Cease, MODY8.
AKLGAVYTEG GFVEGVNKKL SLLGGDSVDI FKGIPFATAK TLENPQRHPG WQGTLKATNF
KKRCLQATIT QDNTYGQEDC LYLNIWVPQG RKQVSHNLPV MVWIYGGAFL MGSGQGANFL
KNYLYDGEEI ATRGNVIVVT FNYRVGPLGF LSTGDANLPG NFGLRDQHMA IAWVKRNIAA
FGGDPDNITI FGESAGAASV SLQTLSPYNK GLIRRAISQS GMALSPWAIQ KNPLFWAKTI
AKKVGCPTED TGKMAACLKI TDPRALTLAY KLPVKKQEYP VVHYLAFIPV IDGDFIPDDP
INLYNNTADI DYIAGINNMD GHLFATIDVP AVDKTKQTVT EEDFYRLVSG HTVAKGLKGA
QATFDIYTES WAQDPSQENM KKTVVAFETD VLFLIPTEIA LAQHKAHAKS AKTYSYLFSH
PSRMPIYPKW MGADHADDLQ YVFGKPFATP LGYRPQDRAV SKAMIAYWTN FARSGDPNMG
NSPVPTHWYP YTLENGNYLD ITKTITSASM KEHLREKFLK FWAVTFEVLP TVTGDQDTLT
PPEDDSEVAP DPPSDDSQVV PVPPTDDSVE AQMPATIGFH HHHHH
Product Science Overview
Carboxyl Ester Lipase (CEL), also known as bile salt-stimulated lipase, is an enzyme with significant lipolytic capabilities. It is capable of hydrolyzing a variety of substrates, including cholesteryl esters, acylglycerols, and ceramide . This enzyme is highly expressed by pancreatic acinar cells and is secreted into the gastrointestinal tract, where it plays a crucial role in the digestion of dietary lipids .
CEL belongs to the Type-B carboxyl esterase/lipase family of enzymes. It possesses a catalytic triad consisting of serine, histidine, and aspartate, which enables it to hydrolyze both ester and amide bonds . The enzyme’s active site is partly shielded by a surface loop, which is controlled by the carboxyl terminus of the enzyme . Bile salt binding to the loop domain frees the active site, allowing accessibility by water-insoluble substrates .
Recombinant Mouse Carboxyl Ester Lipase is produced in various expression systems, including mouse myeloma cell lines and Sf9 Baculovirus cells . The recombinant protein is often tagged with a 6-His tag at the C-terminus to facilitate purification . The recombinant form is typically supplied as a sterile, filtered solution and is stored under specific conditions to maintain stability and activity .
Recombinant Mouse Carboxyl Ester Lipase is used in various research applications, including studies on lipid metabolism, enzyme kinetics, and digestive processes. Its ability to hydrolyze a wide range of substrates makes it a valuable tool for understanding the biochemical pathways involved in lipid digestion and absorption .
