Recombinant Human CES2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1223

Recombinant Human CES2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1223
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Product Overview

Tag His
Host Species Human
Accession O00748
Synonym CE-2, CES2A1, iCE, PCE-2
Background Carboxylesterase 2 (CES2) is a member of the carboxylesterase family and belongs to the multigene family. Carboxylesterase 2 is responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and beroin. It also serves to hydrolyze long-chain fatty acid esters and thioesters. It is speculated that carboxylesterases may play a role in lipid metabolism and the blood-brain barrier system and together with isform 1, are a serine esterase involved in both drug metabolism and activation. Human carboxylesterase 2 is commonly expressed in tumor tissues and irinotecan, a topoisomerase I inhibitor commonly used in the treatment of many solid tumors.
Description A DNA sequence encoding the human CES2 isoform 1 (O00748-1) (Met 1-Leu 559) was expressed, with a C-terminal His tag.
Source HEK293
Predicted N Terminal Gln 27
AA Sequence Met 1-Leu 559
Molecular Weight The secreted recombinant human CES2 comprises 544 a.a. with a predicted molecular mass of 60.4 kDa, as estimated in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 50mM NaAc, 150mM NaCl, 10% Glycerol, pH 5.5.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine. Hydrolyzes aspirin, substrates with large alcohol group and small acyl group and endogenous lipids such as triacylglycerol. Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins.
Subcellular Location Endoplasmic reticulum lumen.
Protein Families Type-B carboxylesterase/lipase family
Database References
Tissue Specificity Preferentially expressed in intestine with moderate expression in liver. Within the intestine, highest expression is found in small intestine with lower expression in colon and rectum.

Gene Functions References

  1. SNPs in CDA and CES2 were associated with benefit from the addition of capecitabine to chemotherapy in metastatic breast cancer patients. PMID: 28827188
  2. Results revealed that most of the colorectal cancer specimens showed a considerable reduction in CES2 expression compared with adjacent normal tissue independently of p53. PMID: 29651325
  3. Anordrin is predominantly catalyzed by CES1 and CES2 to generate the main active metabolite, anordiol. PMID: 28532270
  4. These data suggest that infants younger than 3 weeks of age would exhibit significantly lower CES1- and CES2-dependent metabolic clearance compared with older individuals. PMID: 26825642
  5. Carboxylesterase 2 possesses triglyceride and diacylglycerol lipase activities and displayed an inverse correlation with HOMA-IR and hepatic diacylglycerol concentrations in humans. PMID: 28099843
  6. has triglyceride hydrolase activity; as a result, gain of hepatic CES2 function increases fatty acid oxidation and inhibits lipogenesis, whereas loss of hepatic CES2 stimulates lipogenesis by inducing endoplasmic reticulum stress PMID: 26806650
  7. Plasma cells are strong producers of CES-2 in intestinal inflammation and cancer and may be involved in metabolic activation of ester-containing prodrugs. PMID: 27149931
  8. Data show that carboxylesterase 2 (CES2A1) is the primary mediator of carboxylesterase (CES) substrates in the enterocytes. PMID: 28285137
  9. Findings suggest that CES2 expression and activity, by mediating the intratumoral activation of irinotecan, is a contributor to FOLFIRINOX sensitivity in pancreatic cancer. PMID: 26025324
  10. In the liver and duodenum, CES2 mRNA expression increased and exhibited a postnatal surge. PMID: 25724353
  11. After oral administration of dabigatran etexilate to humans, DABE is hydrolyzed by intestinal CES2 to the intermediate M2 metabolite followed by hydrolysis of M2 to DAB in the liver by CES1. PMID: 24212379
  12. expression of CES2, UGTA1A1, and GUSB varies in colorectal pathology tissues and that the expression of CES2 is somewhat related to tumor staging. PMID: 24195516
  13. Variations in CES2 in the promoter region, may alter rifampicin metabolism by affecting expression of the gene PMID: 23471941
  14. CES2 RNA expression was observed in neuroblastoma cells, and its expression in neuroblastoma cell lines was positively correlated with sensitivity to CPT-11 and apoptosis after CPT-11 exposure in vitro PMID: 23480903
  15. tested the hypothesis that an individual's CES phenotype can be characterized by reporter substrates/probes that interrogate native CES1 and CES2 activities in liver and immunoblotting methods PMID: 22525521
  16. Report CES2 mediated hydrolysis of heroin, cocaine and CPT-11. PMID: 20649590
  17. A comparison of the substrate specificity of CES1 versus CES2 reveals broad but distinct substrate preferences. PMID: 19508181
  18. The multiple promoters in the CES2 gene were characterized. PMID: 12835618
  19. Single-nucleotide polymorphism in carboxylesterase 2 is associated with reduced mRNA expression in colorectal tumors PMID: 15475243
  20. analysis of single nucleotide polymorphisms and haplotype structure of the human carboxylesterase 2 gene PMID: 15475733
  21. human carboxylesterase 2 gene presents several polymorphisms, none of which seems to be involved in significant variations in protein activity PMID: 15592324
  22. TFF-1 is lost late in the progression from Barrett's Esophagus to adenocarcinoma, while CES-2 is upregulated PMID: 15967118
  23. in diffuse large B-cell lymphoma, molecular alterations in ice, bcl-2, c-myc and p53 are present in hematopoietic cells from bone marrow as well as in primitive hematopoietic progenitors PMID: 16690525
  24. p53 directly regulates CES-2 expression in a colonic cancer cell line. PMID: 16963839
  25. 830C>G single nucleotide polymorphism of CES2 is unlikely to have significant functional consequences on CES2 expression, activity or function PMID: 17483951
  26. IL-6 alters the cellular responsiveness to clopidogrel, irinotecan, and oseltamivir by suppressing the expression of CES2. PMID: 17537833
  27. In a Japanese population, CES2 haplotypes and a defective allele were associated with a decrease in enzyme levels or activity. Pharmacokinetics of irinotecan was evaluated in cancer patients. PMID: 17640957
  28. comparative analysis of CES1 and CES2 in liver and small intestine of humans, monkeys, dogs, rabbits and rats PMID: 17764701
  29. Carboxylesterase 2 is downregulated in colorectal cancer following progression of the disease PMID: 18259949
  30. Carboxylesterase 1A2 has been isolated and determined to be identical to carboxylesterase 1A1 except for exon 1 and the 5' regulatory element. PMID: 18305377
  31. an association between a polymorphism in the CES2 gene and the efficacy of capecitabine has been described PMID: 18473752
  32. pharmacogenomic characterization of human carboxylesterase 1A1, 1A2, and 1A3 genes PMID: 18794728
  33. Carboxylesterases play critical roles in drug metabolism and insecticide detoxication; findings show large variability among different age groups or even within the same age group. PMID: 18983829
  34. serum carboxylesterase-2 level might be a potential marker in the diagnosis of the early stage ovarian cancer. PMID: 19856659


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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