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Mouse Anti-CEL Recombinant Antibody (3C8) (CBMAB-C5830-LY)

This product is antibody recognizes CEL. The antibody 3C8 immunoassay techniques such as: ELISA, IF, WB.
See all CEL antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
3C8
Antibody Isotype
IgG1, κ
Application
ELISA, IF, WB

Basic Information

Immunogen
Partial recombinant protein corresponding to aa378-477 from human CEL (AAH42510) with GST tag. MW of the GST tag alone is 26kD
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
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
> 95% Purity determined by SDS-PAGE.
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
Carboxyl Ester Lipase
Introduction
The protein encoded by this gene is a glycoprotein secreted from the pancreas into the digestive tract and from the lactating mammary gland into human milk. The physiological role of this protein is in cholesterol and lipid-soluble vitamin ester hydrolysis and absorption. This encoded protein promotes large chylomicron production in the intestine. Also its presence in plasma suggests its interactions with cholesterol and oxidized lipoproteins to modulate the progression of atherosclerosis. In pancreatic tumoral cells, this encoded protein is thought to be sequestrated within the Golgi compartment and is probably not secreted. This gene contains a variable number of tandem repeat (VNTR) polymorphism in the coding region that may influence the function of the encoded protein. [provided by RefSeq, Jul 2008]
Entrez Gene ID
1056
UniProt ID
P19835
Alternative Names
Carboxyl Ester Lipase; Bile Salt-Stimulated Lipase; Cholesterol Esterase; Sterol Esterase; Bucelipase; BSSL; BAL; Carboxyl Ester Lipase (Bile Salt-Stimulated Lipase); Bile Salt-Dependent Lipase, Oncofetal Isoform; Fetoacinar Pancreatic Protein; Lysophospholipase, Pancreatic; Pancreatic Lysophospholipase; Bile Salt-Activated Lipase;
Function
Catalyzes the hydrolysis of a wide range of substrates including cholesteryl esters, phospholipids, lysophospholipids, di- and tri-acylglycerols, and fatty acid esters of hydroxy fatty acids (FAHFAs) (PubMed:8471055, PubMed:27509211, PubMed:10220579, PubMed:27650499).
Preferentially hydrolyzes FAHFAs with the ester bond further away from the carboxylate. Unsaturated FAHFAs are hydrolyzed more quickly than saturated FAHFAs (By similarity).
Has an essential role in the complete digestion of dietary lipids and their intestinal absorption, along with the absorption of fat-soluble vitamins (PubMed:8471055, PubMed:27509211, PubMed:10220579, PubMed:27650499).
Biological Process
Ceramide catabolic process Source: Ensembl
Chemical synaptic transmission Source: GO_Central
Cholesterol catabolic process Source: UniProtKB
Fatty acid catabolic process Source: UniProtKB
Intestinal cholesterol absorption Source: UniProtKB
Intestinal lipid catabolic process Source: UniProtKB
Lipid digestion Source: Reactome
Lipid metabolic process Source: UniProtKB
Modulation of chemical synaptic transmission Source: GO_Central
Neuron cell-cell adhesion Source: GO_Central
Pancreatic juice secretion Source: UniProtKB
Postsynaptic membrane assembly Source: GO_Central
Presynaptic membrane assembly Source: GO_Central
Protein esterification Source: UniProtKB
Synaptic vesicle endocytosis Source: GO_Central
Cellular Location
Secreted
Involvement in disease
Maturity-onset diabetes of the young 8 with exocrine dysfunction (MODY8): The disease is caused by variants affecting the gene represented in this entry. Single base deletions in the VNTR-region, that result in frame shift and protein truncation, have been identified as disease causing variants in MODY8 families (PubMed:16369531). An autosomal dominant form of diabetes characterized by a primary defect in insulin secretion, exocrine pancreatic dysfunction, altered pancreatic morphology, recurrent abdominal pain, and fecal elastase deficiency. Disease onset is at less than 25 years of age.
PTM
N- and O-glycosylated.

Pellegrini, S., Pipitone, G. B., Cospito, A., Manenti, F., Poggi, G., Lombardo, M. T., ... & Piemonti, L. (2021). Generation of β Cells from iPSC of a MODY8 Patient with a Novel Mutation in the Carboxyl Ester Lipase (CEL) Gene. The Journal of Clinical Endocrinology & Metabolism, 106(5), e2322-e2333.

Gravdal, A., Xiao, X., Cnop, M., El Jellas, K., Johansson, S., Njølstad, P. R., ... & Fjeld, K. (2021). The position of single-base deletions in the VNTR sequence of the carboxyl ester lipase (CEL) gene determines proteotoxicity. Journal of Biological Chemistry, 296.

Dalva, M., Lavik, I. K., El Jellas, K., Gravdal, A., Lugea, A., Pandol, S. J., ... & Molven, A. (2020). Pathogenic carboxyl ester lipase (CEL) variants interact with the normal CEL protein in pancreatic cells. Cells, 9(1), 244.

Qiu, Y., Sun, S., Yu, X., Zhou, J., Cai, W., & Qian, L. (2020). Carboxyl ester lipase is highly conserved in utilizing maternal supplied lipids during early development of zebrafish and human. Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids, 1865(6), 158663.

Khatua, B., Trivedi, R. N., Noel, P., Patel, K., Singh, R., de Oliveira, C., ... & Singh, V. P. (2019). Carboxyl ester lipase may not mediate lipotoxic injury during severe acute pancreatitis. The American journal of pathology, 189(6), 1226-1240.

Oracz, G., Kujko, A. A., Fjeld, K., Wertheim-Tysarowska, K., Adamus-Białek, W., Steine, S. J., ... & Rygiel, A. M. (2019). The hybrid allele 1 of carboxyl-ester lipase (CEL-HYB1) in Polish pediatric patients with chronic pancreatitis. Pancreatology, 19(4), 531-534.

Cui, Y., Jiao, Y., Wang, K., He, M., & Yang, Z. (2019). A new prognostic factor of breast cancer: High carboxyl ester lipase expression related to poor survival. Cancer genetics, 239, 54-61.

Johansson, B. B., Fjeld, K., El Jellas, K., Gravdal, A., Dalva, M., Tjora, E., ... & Molven, A. (2018). The role of the carboxyl ester lipase (CEL) gene in pancreatic disease. Pancreatology, 18(1), 12-19.

El Jellas, K., Johansson, B. B., Fjeld, K., Antonopoulos, A., Immervoll, H., Choi, M. H., ... & Molven, A. (2018). The mucinous domain of pancreatic carboxyl-ester lipase (CEL) contains core 1/core 2 O-glycans that can be modified by ABO blood group determinants. Journal of Biological Chemistry, 293(50), 19476-19491.

Dalva, M., El Jellas, K., Steine, S. J., Johansson, B. B., Ringdal, M., Torsvik, J., ... & Molven, A. (2017). Copy number variants and VNTR length polymorphisms of the carboxyl-ester lipase (CEL) gene as risk factors in pancreatic cancer. Pancreatology, 17(1), 83-88.

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

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