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Rabbit Anti-ACSL1 Recombinant Antibody (V2-179443) (CBMAB-A0750-YC)

Provided herein is a Rabbit monoclonal antibody against Human Acyl-CoA Synthetase Long Chain Family Member 1. The antibody can be used for immunoassay techniques, such as WB, IP.
See all ACSL1 antibodies
Published Data
Rabbit Anti-ACSL1 Recombinant Antibody (D2H5) (CBMAB-A0750-YC) in WB
Immunoblot analysis of acyl-CoA ligase (ACSL) . ...View More
Lizardo, K., Ayyappan, J. P., Oswal, N., Weiss, L. M., Scherer, P. E., & Nagajyothi, J. F. (2021). Fat tissue regulates the pathogenesis and severity of cardiomyopathy in murine chagas disease. PLoS neglected tropical diseases, 15(4), e0008964.

Summary

Host Animal
Rabbit
Specificity
Human, Mouse, Rat, Monkey
Clone
V2-179443
Antibody Isotype
IgG
Application
WB, IP

Basic Information

Immunogen
Synthetic peptide corresponding to residues surrounding Ala257 of human ACSL1 protein.
Specificity
Human, Mouse, Rat, Monkey
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:1,000
IP1:50

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

Buffer
HEPES, pH 7.5, 100 µg/ml BSA, 50% glycerol
Preservative
0.02% sodium azide
Concentration
Batch dependent
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
acyl-CoA synthetase long-chain family member 1
Introduction
ACSL1 is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA
Entrez Gene ID
Human2180
Mouse14081
Rat25288
Monkey694871
UniProt ID
HumanP33121
MouseP41216
RatP18163
MonkeyH2QQI4
Alternative Names
Acyl-CoA Synthetase Long Chain Family Member 1; Fatty-Acid-Coenzyme A Ligase, Long-Chain 2; Long-Chain Fatty-Acid-Coenzyme A Ligase 1; Long-Chain Fatty Acid-CoA Ligase 2; Long-Chain Acyl-CoA Synthetase 1; Long-Chain Acyl-CoA Synthetase 2; Lignoceroyl-CoA
Function
Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate. Preferentially activates arachidonate than epoxyeicosatrienoic acids (EETs) or hydroxyeicosatrienoic acids (HETEs) (By similarity).
Biological Process
Adiponectin-activated signaling pathway
Alpha-linolenic acid metabolic process
Fatty acid transport
Linoleic acid metabolic process
Lipid biosynthetic process
Long-chain fatty acid import into cell
Long-chain fatty acid metabolic process
Long-chain fatty-acyl-CoA biosynthetic process
Positive regulation of cold-induced thermogenesis
Positive regulation of long-chain fatty acid import across plasma membrane
Positive regulation of protein serine/threonine kinase activity
Regulation of metabolic process
Response to drug
Response to nutrient
Response to oleic acid
Response to organic cyclic compound
Triglyceride biosynthetic process
Very long-chain fatty acid metabolic process
Xenobiotic catabolic process
Cellular Location
Peroxisome membrane; Microsome membrane; Endoplasmic reticulum membrane; Mitochondrion outer membrane
Topology
Helical: 25-45 aa
Cytoplasmic: 46-698 aa

Dykstra, H., Fisk, C., LaRose, C., Waldhart, A., Meng, X., Zhao, G., & Wu, N. (2021). Mouse long-chain acyl-CoA synthetase 1 is active as a monomer. Archives of Biochemistry and Biophysics, 700, 108773.

Li, B., Liu, J., Xin, X., Zhang, L., Zhou, J., Xia, C., ... & Yu, H. (2021). MiR-34c promotes hepatic stellate cell activation and Liver Fibrogenesis by suppressing ACSL1 expression. International Journal of Medical Sciences, 18(3), 615.

Huh, J. Y., Reilly, S. M., Abu-Odeh, M., Murphy, A. N., Mahata, S. K., Zhang, J., ... & Saltiel, A. R. (2020). TANK-Binding Kinase 1 Regulates the Localization of Acyl-CoA Synthetase ACSL1 to Control Hepatic Fatty Acid Oxidation. Cell Metabolism, 32(6), 1012-1027.

Guo, L., Lu, J., Gao, J., Li, M., Wang, H., & Zhan, X. (2020). The function of SNHG7/miR‐449a/ACSL1 axis in thyroid cancer. Journal of cellular biochemistry, 121(10), 4034-4042.

Singh, A. B., Dong, B., Xu, Y., Zhang, Y., & Liu, J. (2019). Identification of a novel function of hepatic long-chain acyl-CoA synthetase-1 (ACSL1) in bile acid synthesis and its regulation by bile acid-activated farnesoid X receptor. Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids, 1864(3), 358-371.

Roelands, J., Garand, M., Hinchcliff, E., Ma, Y., Shah, P., Toufiq, M., ... & Chaussabel, D. (2019). Long-chain acyl-CoA synthetase 1 role in sepsis and immunity: perspectives from a parallel review of public transcriptome datasets and of the literature. Frontiers in immunology, 10, 2410.

Yang, G., Wang, Y., Feng, J., Liu, Y., Wang, T., Zhao, M., ... & Zhang, X. (2017). Aspirin suppresses the abnormal lipid metabolism in liver cancer cells via disrupting an NFκB-ACSL1 signaling. Biochemical and biophysical research communications, 486(3), 827-832.

Wang, Y., Cai, X., Zhang, S., Cui, M., Liu, F., Sun, B., ... & Ye, L. (2017). HBXIP up-regulates ACSL1 through activating transcriptional factor Sp1 in breast cancer. Biochemical and biophysical research communications, 484(3), 565-571.

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

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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.).

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