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Mouse Anti-FADS1 (AA 1-100) Recombinant Antibody (CBXF-0265) (CBMAB-F0274-CQ)

This product is a mouse antibody that recognizes FADS1 (AA 1-100). The antibody CBXF-0265 can be used for immunoassay techniques such as: ELISA, WB.
See all FADS1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBXF-0265
Antibody Isotype
IgG2a
Application
ELISA, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG2a
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
Buffer
PBS, pH 7.2
Preservative
0.09% sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 1-100

Target

Full Name
fatty acid desaturase 1
Introduction
The protein encoded by this gene is a member of the fatty acid desaturase (FADS) gene family. Desaturase enzymes regulate unsaturation of fatty acids through the introduction of double bonds between defined carbons of the fatty acyl chain. FADS family members are considered fusion products composed of an N-terminal cytochrome b5-like domain and a C-terminal multiple membrane-spanning desaturase portion, both of which are characterized by conserved histidine motifs. This gene is clustered with family members FADS1 and FADS2 at 11q12-q13.1; this cluster is thought to have arisen evolutionarily from gene duplication based on its similar exon/intron organization.
Entrez Gene ID
3992
UniProt ID
O60427
Alternative Names
Fatty Acid Desaturase 1; Delta(5) Desaturase; Delta-5 Desaturase; FADSD5; D5D; Linoleoyl-CoA Desaturase (Delta-6-Desaturase)-Like 1; Delta(5) Fatty Acid Desaturase;
Research Area
Isoform 1:
Acts as a front-end fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 5 located between a preexisting double bond and the carboxyl end of the fatty acyl chain. Involved in biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors. Specifically, desaturates dihomo-gamma-linoleoate (DGLA) (20:3n-6) and eicosatetraenoate (ETA) (20:4n-3) to generate arachidonate (AA) (20:4n-6) and eicosapentaenoate (EPA) (20:5n-3), respectively (PubMed:10601301, PubMed:10769175).

As a rate limiting enzyme for DGLA (20:3n-6) and AA (20:4n-6)-derived eicosanoid biosynthesis, controls the metabolism of inflammatory lipids like prostaglandin E2, critical for efficient acute inflammatory response and maintenance of epithelium homeostasis. Contributes to membrane phospholipid biosynthesis by providing AA (20:4n-6) as a major acyl chain esterified into phospholipids. In particular, regulates phosphatidylinositol-4,5-bisphosphate levels, modulating inflammatory cytokine production in T-cells (By similarity).

Also desaturates (11E)-octadecenoate (trans-vaccenoate)(18:1n-9), a metabolite in the biohydrogenation pathway of LA (18:2n-6) (By similarity).

Isoform 2:
Does not exhibit any catalytic activity toward 20:3n-6, but it may enhance FADS2 activity.
Biological Process
Alpha-linolenic acid metabolic process Source: Reactome
Cell-cell signaling Source: UniProtKB
Cellular response to starvation Source: UniProtKB
Icosanoid biosynthetic process Source: UniProtKB
Linoleic acid metabolic process Source: Reactome
Long-chain fatty acid biosynthetic process Source: MGI
Phospholipid biosynthetic process Source: UniProtKB
Regulation of cell differentiation Source: UniProtKB
Regulation of transcription, DNA-templated Source: UniProtKB
Unsaturated fatty acid biosynthetic process Source: UniProtKB
Cellular Location
Isoform 1: Endoplasmic reticulum membrane; Mitochondrion
Isoform 2: Endoplasmic reticulum membrane
Topology
Cytoplasmic: 1-121
Helical: 122-142
Lumenal: 143-145
Helical: 146-170
Cytoplasmic: 171-267
Helical: 268-288
Lumenal: 289-305
Helical: 306-326
Cytoplasmic: 327-444

Zhou, C., Zhang, W., Lin, H., Zhang, L., Wu, F., Wang, Y., ... & Huang, Z. (2022). Effect of theaflavin-3, 3'-digallate on leptin-deficient induced nonalcoholic fatty liver disease might be related to lipid metabolism regulated by the Fads1/PPARδ/Fabp4 axis and gut microbiota. Frontiers in pharmacology, 13, 925264-925264.

Knez, M., Pantovic, A., Tako, E., & Boy, E. (2022). FADS1 and FADS2 as biomarkers of Zn status–a systematic review and meta-analysis. Critical Reviews in Food Science and Nutrition, 1-19.

Zhao, R., Tian, L., Zhao, B., Sun, Y., Cao, J., Chen, K., ... & Liu, M. (2020). FADS1 promotes the progression of laryngeal squamous cell carcinoma through activating AKT/mTOR signaling. Cell death & disease, 11(4), 1-14.

Reynolds, L. M., Dutta, R., Seeds, M. C., Lake, K. N., Hallmark, B., Mathias, R. A., ... & Chilton, F. H. (2020). FADS genetic and metabolomic analyses identify the∆ 5 desaturase (FADS1) step as a critical control point in the formation of biologically important lipids. Scientific reports, 10(1), 1-12.

Lian, H., Xie, P., Yin, N., Zhang, J., Zhang, X., Li, J., & Zhang, C. (2019). Linc00460 promotes osteosarcoma progression via miR-1224-5p/FADS1 axis. Life sciences, 233, 116757.

Koletzko, B., Reischl, E., Tanjung, C., Gonzalez-Casanova, I., Ramakrishnan, U., Meldrum, S., ... & Demmelmair, H. (2019). FADS1 and FADS2 polymorphisms modulate fatty acid metabolism and dietary impact on health. Annual review of nutrition, 39, 21-44.

Yuan, S., Bäck, M., Bruzelius, M., Mason, A. M., Burgess, S., & Larsson, S. (2019). Plasma phospholipid fatty acids, FADS1 and risk of 15 cardiovascular diseases: a Mendelian randomisation study. Nutrients, 11(12), 3001.

Gromovsky, A. D., Schugar, R. C., Brown, A. L., Helsley, R. N., Burrows, A. C., Ferguson, D., ... & Brown, J. M. (2018). Δ-5 fatty acid desaturase FADS1 impacts metabolic disease by balancing proinflammatory and proresolving lipid mediators. Arteriosclerosis, thrombosis, and vascular biology, 38(1), 218-231.

He, Z., Zhang, R., Jiang, F., Zhang, H., Zhao, A., Xu, B., ... & Hu, C. (2018). FADS1-FADS2 genetic polymorphisms are associated with fatty acid metabolism through changes in DNA methylation and gene expression. Clinical epigenetics, 10(1), 1-13.

Lopes-Marques, M., Kabeya, N., Qian, Y., Ruivo, R., Santos, M. M., Venkatesh, B., ... & Monroig, Ó. (2018). Retention of fatty acyl desaturase 1 (fads1) in Elopomorpha and Cyclostomata provides novel insights into the evolution of long-chain polyunsaturated fatty acid biosynthesis in vertebrates. BMC evolutionary biology, 18(1), 1-9.

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

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