Sign in or Register   Sign in or Register
  |  

Mouse Anti-CES1 Recombinant Antibody (A106) (CBMAB-AP11706LY)

The product is antibody recognizes CES1. The antibody A106 immunoassay techniques such as: ELISA, WB.
See all CES1 antibodies

Summary

Host Animal
Mouse
Specificity
P. aeruginosa
Clone
A106
Antibody Isotype
IgG1
Application
ELISA, WB

Basic Information

Immunogen
Recombinant full length Pseudomonas aeruginosa Metallothionein protein
Specificity
P. aeruginosa
Antibody Isotype
IgG1
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Purity
Affinity purity
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Carboxylesterase 1
Introduction
This gene encodes a member of the carboxylesterase large family. The family members are responsible for the hydrolysis or transesterification of various xenobiotics, such as cocaine and heroin, and endogenous substrates with ester, thioester, or amide bonds. They may participate in fatty acyl and cholesterol ester metabolism, and may play a role in the blood-brain barrier system. This enzyme is the major liver enzyme and functions in liver drug clearance. Mutations of this gene cause carboxylesterase 1 deficiency. Three transcript variants encoding three different isoforms have been found for this gene. [provided by RefSeq, Jun 2010]
Alternative Names
Carboxylesterase 1; Carboxylesterase 1 (Monocyte/Macrophage Serine Esterase 1); Human Monocyte/Macrophage Serine Esterase 1; Methylumbelliferyl-Acetate Deacetylase 1; Monocyte/Macrophage Serine Esterase; Brain Carboxylesterase HBr1; Triacylglycerol Hydrolase; Cocaine Carboxylesterase; Retinyl Ester Hydrolase; Serine Esterase 1; EC 3.1.1.1; Egasyn; HCE-1; ACAT; CE-1; CES2;
Function
Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs (PubMed:7980644, PubMed:9169443, PubMed:9490062, PubMed:18762277).
Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester (PubMed:7980644, PubMed:9169443, PubMed:9490062, PubMed:18762277).
Hydrolyzes the methyl ester group of cocaine to form benzoylecgonine (PubMed:7980644).
Catalyzes the transesterification of cocaine to form cocaethylene (PubMed:7980644).
Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate (PubMed:7980644).
Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins (PubMed:21049984).
Hydrolyzes cellular cholesteryl esters to free cholesterols and promotes reverse cholesterol transport (RCT) by facilitating both the initial and final steps in the process (PubMed:18762277, PubMed:16024911, PubMed:11015575, PubMed:16971496).
First of all, allows free cholesterol efflux from macrophages to extracellular cholesterol acceptors and secondly, releases free cholesterol from lipoprotein-delivered cholesteryl esters in the liver for bile acid synthesis or direct secretion into the bile (PubMed:18762277, PubMed:18599737, PubMed:16971496).
Biological Process
Angiotensin maturation Source: Reactome
Cellular response to cholesterol Source: ARUK-UCL
Cellular response to low-density lipoprotein particle stimulus Source: ARUK-UCL
Cholesterol biosynthetic process Source: BHF-UCL
Cholesterol ester hydrolysis involved in cholesterol transport Source: BHF-UCL
Cholesterol homeostasis Source: ARUK-UCL
Cholesterol metabolic process Source: UniProtKB
Epithelial cell differentiation Source: UniProtKB
Lipid catabolic process Source: GO_Central
Medium-chain fatty acid metabolic process Source: BHF-UCL
Negative regulation of cholesterol storage Source: UniProtKB
Positive regulation of cholesterol efflux Source: UniProtKB
Positive regulation of cholesterol metabolic process Source: UniProtKB
Regulation of bile acid biosynthetic process Source: UniProtKB
Regulation of bile acid secretion Source: UniProtKB
Response to toxic substance Source: ProtInc
Reverse cholesterol transport Source: UniProtKB
Xenobiotic metabolic process Source: Reactome
Cellular Location
Cytoplasm; Endoplasmic reticulum lumen; Lipid droplet. Moves from cytoplasm to lipid droplets upon lipid loading. Associates with lipid droplets independently of triglycerides (TG) content of the droplets and hydrolyzes cholesteryl esters more efficiently from mixed droplets.
PTM
Contains sialic acid.
Cleavage of the signal sequence can occur at 2 positions, either between Trp-17 and Gly-18 or between Gly-18 and His-19.

Na, K., Kim, M., Kim, C. Y., Lim, J. S., Cho, J. Y., Shin, H., ... & Paik, Y. K. (2020). Potential Regulatory Role of Human-Carboxylesterase-1 Glycosylation in Liver Cancer Cell Growth. Journal of Proteome Research, 19(12), 4867-4883.

Her, L., & Zhu, H. J. (2020). Carboxylesterase 1 and precision pharmacotherapy: pharmacogenetics and nongenetic regulators. Drug Metabolism and Disposition, 48(3), 230-244.

Xu, Y., Zhu, Y., Bawa, F. C., Hu, S., Pan, X., Yin, L., & Zhang, Y. (2020). Hepatocyte‐Specific Expression of Human Carboxylesterase 1 Attenuates Diet‐Induced Steatohepatitis and Hyperlipidemia in Mice. Hepatology communications, 4(4), 527-539.

Wang, X., Shi, J., & Zhu, H. J. (2019). Functional study of carboxylesterase 1 protein isoforms. Proteomics, 19(4), 1800288.

Ding, L., Tian, Z., Hou, J., Dou, T., Jin, Q., Wang, D., ... & Ge, G. (2019). Sensing carboxylesterase 1 in living systems by a practical and isoform-specific fluorescent probe. Chinese Chemical Letters, 30(3), 558-562.

Tian, Z., Ding, L., Li, K., Song, Y., Dou, T., Hou, J., ... & Cui, J. (2019). Rational design of a long-wavelength fluorescent probe for highly selective sensing of carboxylesterase 1 in living systems. Analytical chemistry, 91(9), 5638-5645.

Qian, Y., Wang, X., & Markowitz, J. S. (2019). In vitro inhibition of carboxylesterase 1 by major cannabinoids and selected metabolites. Drug Metabolism and Disposition, 47(5), 465-472.

Neuvonen, M., Tarkiainen, E. K., Tornio, A., Hirvensalo, P., Tapaninen, T., Paile‐Hyvärinen, M., ... & Niemi, M. (2018). Effects of genetic variants on carboxylesterase 1 gene expression, and clopidogrel pharmacokinetics and antiplatelet effects. Basic & clinical pharmacology & toxicology, 122(3), 341-345.

Xu, J., Xu, Y., Xu, Y., Yin, L., & Zhang, Y. (2017). Global inactivation of carboxylesterase 1 (Ces1/Ces1g) protects against atherosclerosis in Ldlr−/− mice. Scientific reports, 7(1), 1-12.

Wang, X., Rida, N., Shi, J., Wu, A. H., Bleske, B. E., & Zhu, H. J. (2017). A comprehensive functional assessment of carboxylesterase 1 nonsynonymous polymorphisms. Drug Metabolism and Disposition, 45(11), 1149-1155.

Ask a question We look forward to hearing from you.
0 reviews or Q&As

Purchasing FAQs
Technical FAQs

Loading...
Have you used Mouse Anti-CES1 Recombinant Antibody (A106)?
Submit a review and get a Coupon or an Amazon gift card. 20% off Coupon $30 eGift Card
Submit a review
Loading...
For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

Online Inquiry

Documents

Contact us

  • Tel: (USA)
  • (UK)
  • Fax:
  • Email:

Submit A Review

Go to
Compare